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Enzyme Nomenclature
Information on EC 1.1.1.1 - alcohol dehydrogenase
Word Map on EC 1.1.1.1
- 1.1.1.1
- acetaldehyde
- hepatic
- drosophila
- pyruvate
- disulfiram
- lactate
- melanogaster
- catalase
- horse
- zinc
- methanol
- hepatocytes
-
ingest
- dinucleotide
- nicotinamide
-
retinoic
- pyrazole
- nadp+
-
intoxication
-
ethanol-induced
-
semialdehyde
- retinal
- injury
- stomach
- malate
-
abuse
- maize
-
poison
-
carcinogen
-
alcohol-induced
- benzaldehyde
- cyp2e1
-
allozymes
- mobilis
-
hydride
-
flush
- butanol
- cyclophosphamide
- acrolein
-
self-renewal
-
nadp+-dependent
-
drinker
- ichthyosis
-
first-pass
- diethyldithiocarbamate
- synthesis
- medicine
-
stem-like
-
chaperone-like
- etoh
- biotechnology
-
ethanol-treated
- pargyline
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The enzyme appears in viruses and cellular organisms
topEC NUMBER 
COMMENTARY 
1.1.1.1
-
RECOMMENDED NAME
GeneOntology No.
alcohol dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a secondary alcohol + NAD+ = a ketone + NADH + H+
-
-
-
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
ordered bi bi mechanism with cofactor adding first to form a binary enzyme complex
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
isoenzyme EE and SS: ordered bi bi mechanism
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
Theorell-Chance mechanism
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
kinetic mechanism is random for ethanol oxidation and compulsory ordered for acetaldehyde reduction
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
ordered bi-bi mechanism
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
rapid equilibrium random mechanism
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
rapid equilibrium random mechanism
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
Theorell-Chance mechanism
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
Theorell-Chance mechanism
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
oxidizes ethanol in an ordered bi-bi mechanism with NAD+ as the first substrate fixed
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
compulsory-order mechanism with the rate-limiting step being the dissociation of the product enzyme-NAD+ complex
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
mechanism is predominantly ordered with ethanol, but partially random with butanol
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
mechanism is predominantly ordered with ethanol, but partially random with butanol
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
Ser48 is involved in catalysis, isozyme gamma(2)gamma(2)
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
ordered bibi mechanism, structural and functional implications of amino acid residue 47
a primary alcohol + NAD+ = an aldehyde + NADH + H+
reaction mechanism, His51 is involved, but not essential, in catalysis facilitating the deprotonation of the hydroxyl group of water or alcohol ligated to the catalytic zinc
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
sequential reaction mechanism
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
ordered sequential bibi reaction mechanism, modeling of oxidation kinetic mechanism
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
detailed determination of the reaction and kinetic mechanisms, active site structure and determination of amino acid residues involved in catalysis, 3 isozymes
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
class IV alcohol dehydrogenase also functions as retinol dehydrogenase, reaction and kinetic mechanism: asymmetric rapid equilibrium random mechanism with 2 dead-end ternary complexes fro retinol oxidation and a rapid equilibrium ordered mechanism with one dead-end ternary complex for retinal reduction, a unique mechanistic form fro zinc-containing ADH in the medium chain dehydrogenase/reductase superfamily of enzymes
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
the catalytic triad consists of Cys44, His67, and Cys154, active site structure
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
catalytic mechanism involves a proton relay modulated by the coupled ionization of the active site Lys155/Tyr151 pair, and a NAD+ ribose 2'-OH switch, other active site residues are Ser138 and Trp144, ionization properties, substrate binding, overview
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
oxidizes ethanol in an ordered bi-bi mechanism with NAD+ as the first substrate fixed
-
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
the catalytic triad consists of Cys44, His67, and Cys154, active site structure
-
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
sequential reaction mechanism
-
-
a primary alcohol + NAD+ = an aldehyde + NADH + H+
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
reduction
-
-
-
-
redox reaction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
SYSTEMATIC NAME
IUBMB Comments
alcohol:NAD+ oxidoreductase
A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
CAS REGISTRY NUMBER
COMMENTARY
9031-72-5
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cationic pyrazole-sensitive isoenzyme, anodic pyrazole-sensitive isoenzyme and cathionic pyrazole-in sensitive isoenzyme
-
-
i.e. Pichia angusta, HpADH3 is not the major ADH in strain DL-1, gene ADH3
UniProt
i.e. Pichia angusta, HpADH3 is not the major ADH in strain DL-1, gene ADH3
UniProt
-
285581, 285582, 285584, 285585, 285586, 285587, 285588, 285589, 285591, 285592, 285594, 285595, 285609, 285610, 285641, 285647, 285648, 285653, 285657, 655206, 655233, 668487, 685703, 695889, 697215, 697660
-
-
-
-
-
class I isoenzymes: alpha,gamma2, gamma2gamma2, alpha,gamma1, alpha,beta1, beta1,gamma2, gamma1,gamma1, beta1,gamma1, beta1,beta1
-
-
-
285558, 285641, 285643, 285644, 285645, 285649, 654053, 655735, 655741, 667307, 668532, 669148, 685776, 687134, 687831, 688435, 688657, 688866, 689887, 695705, 696411, 697267, 697658, 735629, 735836, 736534
-
-
-
-
-
-
UniProt
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
-
the enzyme belongs to the short-chain alcohol dehydrogenases
evolution
the class I type enzyme belongs to the medium-chain alcohol dehydrogenases, structural and evolutionary relationships of the pigeon enzyme, phylogenetic tree, overview
evolution
the class III type enzyme belongs to the medium-chain alcohol dehydrogenases, structural and evolutionary relationships of the dogfish enzyme, phylogenetic tree, overview
evolution
alcohol dehydrogenase is a fermentative enzyme that is highly conserved across species, from prokaryotes to fungi, plants, and animals
evolution
-
the enzyme belongs to the short-chain alcohol dehydrogenases
-
evolution
-
alcohol dehydrogenase is a fermentative enzyme that is highly conserved across species, from prokaryotes to fungi, plants, and animals
-
evolution
-
the enzyme ADH3 belongs to the group III alcohol dehydrogenases
-
physiological function
-
different fermentation product yields observed in different ethanol-producing thernophiles that employ the phosphoroclastic pathway for pyruvate metabolism are related to the specific activities and the direction of specific oxidoreductases that control electron flow. Thermoanaerobium brockii extracts contain reversible NAD- and NADP-linked alcohol dehydrogenase activities that are not effectively inhibited by low NAD(P) or ethanol
physiological function
Adh1 is the primary alcohol dehydrogenase responsible for the production of ethanol from the reduction of acetaldehyde in Kluyveromyces marxianus
physiological function
-
deletion of the bifunctional alcohol and aldehyde dehydrogenase gene adhE reduces ethanol production by more than 95%. In the deletion strains, fermentation products shift from ethanol to lactate production and result in lower cell density and longer time to reach maximal cell density. The deletion strain additionally contains a point mutation in the lactate dehydrogenase gene, which appears to deregulate its activation by fructose 1,6-bisphosphate, leading to constitutive activation of lactate dehydrogenase
physiological function
deletion of the bifunctional alcohol and aldehyde dehydrogenase gene adhE reduces ethanol production by more than 95%. In the deletion strain, fermentation products shift from ethanol to lactate production and result in lower cell density and longer time to reach maximal cell density. It loses more than 85% of alcohol dehydrogenase activity. Aldehyde dehydrogenase activity does not appear to be affected, although its activity is low in cell extracts. Adding ubiquinone-0 to the aldehyde dehydrogenase assay increases activity in the parent strain but does not increase activity in the adhE deletion strain
physiological function
-
in ethanol-tolerant mutant strain, EA, the tolerant phenotype is primarily due to a mutated bifunctional acetaldehyde-CoA/alcohol dehydrogenase gene (adhE), with a complete loss of NADH-dependent activity and concomitant acquisition of NADPH-dependent activity, which likely affects electron flow in the mutant strain. Mutant adhE allele alone confers increased ethanol tolerance
physiological function
-
Adh1 is the primary alcohol dehydrogenase responsible for the production of ethanol from the reduction of acetaldehyde in Kluyveromyces marxianus
-
physiological function
Ruminiclostridium thermocellum DSM 1237
-
deletion of the bifunctional alcohol and aldehyde dehydrogenase gene adhE reduces ethanol production by more than 95%. In the deletion strains, fermentation products shift from ethanol to lactate production and result in lower cell density and longer time to reach maximal cell density. The deletion strain additionally contains a point mutation in the lactate dehydrogenase gene, which appears to deregulate its activation by fructose 1,6-bisphosphate, leading to constitutive activation of lactate dehydrogenase; in ethanol-tolerant mutant strain, EA, the tolerant phenotype is primarily due to a mutated bifunctional acetaldehyde-CoA/alcohol dehydrogenase gene (adhE), with a complete loss of NADH-dependent activity and concomitant acquisition of NADPH-dependent activity, which likely affects electron flow in the mutant strain. Mutant adhE allele alone confers increased ethanol tolerance
-
physiological function
-
deletion of the bifunctional alcohol and aldehyde dehydrogenase gene adhE reduces ethanol production by more than 95%. In the deletion strain, fermentation products shift from ethanol to lactate production and result in lower cell density and longer time to reach maximal cell density. It loses more than 85% of alcohol dehydrogenase activity. Aldehyde dehydrogenase activity does not appear to be affected, although its activity is low in cell extracts. Adding ubiquinone-0 to the aldehyde dehydrogenase assay increases activity in the parent strain but does not increase activity in the adhE deletion strain
-
additional information
-
ADH1 molecular modeling and molecular dynamics simulations, and comparison to rat ADH5 enzyme, overview
additional information
-
ADH5 molecular modeling and molecular dynamics simulations, and comparison to human ADH1 enzyme, overview
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(-)-carvone + NADH + H+
? + NAD+
1% activity compared to cyclohexanone
-
-
?
(1S,3S)-3-methylcyclohexanol + NAD+
(rac)-3-methylcyclohexanone + NADH + H+
125% activity compared to cyclohexanol
163% activity compared to cyclohexanone
-
r
(2E)-but-2-enal + NADPH + H+
(2E)-but-2-en-1-ol + NADP+
yield 96% after 12 h
-
-
r
(2E)-dec-2-enal + NADPH + H+
(2E)-dec-2-en-1-ol + NADP+
16.7% of the activity with (2E)-but-2-enal, yield 91% after 12 h
-
-
?
(2E)-hex-2-enal + NADPH + H+
(2E)-hex-2-en-1-ol + NADP+
41.7% of the activity with (2E)-but-2-enal, yield 98% after 12 h
-
-
?
(2E)-oct-2-enal + NADPH + H+
(2E)-oct-2-en-1-ol + NADP+
30.2% of the activity with (2E)-but-2-enal, yield 69% after 12 h
plus 27% oct-2-enyl ester
-
?
(6S)-5,6-dihydro-6-methyl-4H-thieno[2,3b]thiopyran-4-one-7,7-dioxide + NADH + H+
(4S,6S)-5,6-dihydro-4-hydroxy-6-methyl-4H-thieno[2,3b]thiopyran-7,7-dioxide + NAD+
-
-
-
-
-
(R)-1-indanol + NAD+
?
62% of activity compared to (S)-1-indanol
-
-
?
(R)-3-methylcyclohexanone + NADH + H+
? + NAD+
2% activity compared to cyclohexanone
-
-
?
(R)-alpha-tetralol + NAD+
?
58% of activity compared to (S)-1-indanol
-
-
?
(R)-alpha-tetralol + NAD+
alpha-tetralone + NADH + H+
-
-
-
r
(S)-1-phenyl-2-propanol + NAD+
phenylacetone + NADH + H+
-
9% activity compared to cyclohexanone
-
r
(S)-2-heptanol + NAD+
2-heptanone + NADH + H+
-
331% of the activity with 2-propanol
-
-
r
(S)-2-hexanol + NAD+
2-hexanone + NADH + H+
-
38% of the activity with 2-propanol
-
-
r
(S)-2-pentanol + NAD+
?
11% of activity compared to (S)-1-indanol
-
-
?
(S)-2-phenylpropanol + NAD+
(S)-2-phenylpropanal + NADH + H+
-
156% of the activity with 2-phenylethanol
-
-
?
(S)-4-phenylbutan-2-ol + NAD+
benzylacetone + NADH + H+
-
3% activity compared to cyclohexanone
-
r
(S)-alpha-tetralol + NAD+
?
12% of activity compared to (S)-1-indanol
-
-
?
(S)-perillylalcohol + NAD+
(S)-perillaldehyde + NADH + H+
52% activity compared to cyclohexanol
-
-
?
(Z)-hex-2-en-1-ol + NAD+
(Z)-hex-2-en-1-one + NADH
-
9.7% of the activity with ethanol
-
-
?
1,1-dichloroacetone + NADH + H+
1,1-dichloropropan-2-ol + NADH
-
1078% of the activity with phenyl trifluoromethyl ketone
-
-
?
1,2-hexanediol + NAD+
?
-
20% of the activity with (S)-N-benzyl-3-pyrrolidinol
-
-
?
1,2-pentanediol + NAD+
?
-
12% of the activity with (S)-N-benzyl-3-pyrrolidinol
-
-
?
1,3-butanediol + NAD+
?
-
39% of the activity with (S)-N-benzyl-3-pyrrolidinol
-
-
?
1-(3-bromophenyl)ethanol + NAD+
1-(3-bromophenyl)ethanone + NADH + H+
315% of the activity with 1-phenylethanol
-
-
?
1-(3-chlorophenyl)ethanol + NAD+
1-(3-chlorophenyl)ethanone + NADH + H+
205% of the activity with 1-phenylethanol
-
-
?
1-(4'-chlorophenyl)ethanol + NAD+
1-(4'-chlorophenyl)ethanone + NADH + H+
-
26% of the activity with (S)-(-)-1-phenylethanol
-
-
?
1-(4'-fluorophenyl)ethanol + NAD+
1-(4'-fluorophenyl)ethanone + NADH + H+
-
45% of the activity with (S)-1-phenylethanol
-
-
r
1-(4-bromophenyl)ethanol + NAD+
1-(4-bromophenyl)ethanone + NADH + H+
167% of the activity with 1-phenylethanol
-
-
?
1-(4-chlorophenyl)ethanol + NAD+
1-(4-chlorophenyl)ethanone + NADH + H+
151% of the activity with 1-phenylethanol
-
-
?
1-(4-methylphenyl)ethanol + NAD+
1-(4-methylphenyl)ethanone + NADH + H+
189% of the activity with 1-phenylethanol
-
-
?
1-(p-tolyl)-ethanol + NAD+
1-(4-methylphenyl)ethanone + NADH + H+
19% activity compared to cyclohexanol
26% activity compared to cyclohexanone
-
?
1-chloro-5-acetylfuro[2,3-c]pyridine + NADH + H+
1-chloro-5-(1-hydroxyethyl)furo[2,3-c]pyridine + NAD+
-
-
-
-
r
1-decalone + NADH + H+
decahydronaphthalen-1-ol + NAD+
85% of the activity compared to 1-phenyl-1,2-propanedione
-
-
?
1-heptanol + NAD+
heptanol + NADH + H+
-
56% of the activity with 2-propanol, in the reverse reaction 755% of the activity with phenyl trifluoromethyl ketone
-
-
r
1-hexanol + NAD+
?
-
15% of the activity with (S)-N-benzyl-3-pyrrolidinol
-
-
?
1-hydroxy-2-butanone + NADH + H+
butane-1,2-diol + NAD+
-
59% of the activity with N-benzyl-3-pyrrolidinone
-
-
?
1-hydroxymethyl-6-methylpyrene + NAD+
1-formyl-6-methylpyrene + NADH + H+
-
-
-
r
1-hydroxymethyl-8-methylpyrene + NAD+
1-formyl-8-methylpyrene + NADH + H+
-
-
-
r
1-octanol + 2 NADP+ + H2O
octanoic acid + 2 NADPH + 2 H+
-
-
-
r
1-octanol + NAD+
1-octanal + NADH + H+
-
6% of activity with N-benzyl-3-pyrrolidinol
-
-
?
1-pentanol + NAD+
pentanal + NADH + H*
-
8% of the activity with (S)-N-benzyl-3-pyrrolidinol
-
-
?
1-phenyl-1,2-ethanediol + NAD+
1-phenyl-2-propanone + NADH + H+
1% activity compared to cyclohexanol
-
-
r
1-phenyl-1,2-propandione + NADH + H+
1-phenyl-2-hydroxy-1-propanone + NAD+
-
146% of the activity with 2,2,2-trifluoroacetophenone
-
-
r
1-phenyl-1,2-propanedione + NADH
?
about 25% of the activity compared to isatin
-
-
?
1-phenyl-1-propanol + NAD+
1-phenyl-1-propanone + NADH + H+
-
59% of the activity with (S)-(-)-1-phenylethanol
-
-
?
1-phenyl-1-propanol + NAD+
1-phenylpropanal + NADH + H+
-
59% of the activity with (S)-1-phenylethanol
-
-
r
1-phenyl-1-propanol + NAD+
?
-
31% of the activity with (S)-N-benzyl-3-pyrrolidinol
-
-
?
1-phenyl-2-propanone + NADH + H+
(S)-1-phenyl-2-propanol + NAD+
-
-
-
-
-
1-phenyl-3-butanone + NADH + H+
1-phenylbutan-3-ol + NAD+
-
353% of the activity with phenyl trifluoromethyl ketone
-
-
?
1-phenylethanol + NAD+
acetophenone + NADH + H+
-
1% activity compared to cyclohexanone
-
?
1-phenylethanol + NADP+
1-phenylethanone + NADPH + H+
-
-
-
?
12-hydroxylauric acid methyl ester + NAD+
12-oxo lauricacid methyl ester + NADH + H+
-
-
product is a key intermediate for biobased polyamide 12 production
-
?
12-oxolauric acid methyl ester + NADH + H+
12-hydroxylauric acid methyl ester + NAD+
-
-
-
-
?
2',3',4',5',6'-pentafluoroacetophenone + NADH + H+
1-(2,3,4,5,6-pentafluorophenyl)ethanol + NAD+
45% of the activity compared to 1-phenyl-1,2-propanedione
-
-
?
2,2'-dichlorobenzil + NADH + H+
1,2-bis(2-chlorophenyl)-2-hydroxyethanone + NAD+
-
-
-
?
2,2,2-trichloroethanol + NAD+
trichloroacetaldehyde + NADH + H+
-
-
-
-
?
2,2,2-trifluoroacetophenone + NADH
2,2,2-trifluoro-1-phenylethanol + NAD+
about 35% of the activity compared to isatin
-
-
?
2,2,2-trifluoroacetophenone + NADPH + H+
(R)-2,2,2-trifluoro-1-phenylethanol + NADP+
180% of the activity with acetoin
-
-
r
2,3'-dichloroacetophenone + NADH + H+
1-(2,3-dichlorophenyl)ethanol + NAD+
-
67% of the activity with phenyl trifluoromethyl ketone
-
-
?
2,3'-dichloroacetophenone + NADH + H+
2-chloro-1-(3-chlorophenyl)ethanol + NAD+
-
-
-
-
r
2,3-butanediol + NAD+
?
-
83% of the activity with (S)-N-benzyl-3-pyrrolidinol
-
-
?
2,3-butanedione + NADH + H+
?
-
activity is 1.6fold higher than with N-benzyl-3-pyrrolidinone
-
-
?
2,3-pentanedione + NADH
? + NADH
-
5.5% of the activity with acetaldehyde
-
-
?
2-(3-fluorobiphenyl-4-yl)propanal + NADH + H+
(S)-2-(3-(fluoro)biphenyl-4-yl)propanol + NAD+
2-(4-trifluoromethylphenyl)propanal + NADH + H+
(S)-2-(4-trifluoromethyl)phenylpropanol + NAD+
-
18 h, 55% yield, 98% enantiomeric excess
-
-
?
2-(6-methoxynaphthalen-2-yl)propanal + NADH + H+
(S)-2-(6-methoxynaphthalen-2-yl)propan-1-ol + NAD+
-
18 h, 96% yield, 98% enantiomeric excess
-
-
?
2-(naphthalen-1-yl)propanal + NADH + H+
(S)-2-(naphthalen-1-yl)propanol + NAD+
-
18 h, 90% yield, 80% enantiomeric excess
-
-
?
2-(naphthalen-2-yl)propanal + NADH + H+
(S)-2-(naphthalen-2-yl)propanol + NAD+
-
18 h, 57% yield, 94% enantiomeric excess
-
-
?
2-acetylpyrrole + NADH + H+
1-(1H-pyrrol-2-yl)ethanol + NAD+
-
70% of activity with N-benzyl-3-pyrrolidinone
-
-
?
2-butanone + NADH + H+
butan-2-ol + NAD+
-
2.8fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
2-chloroacetophenone + NADH + H+
1-(2-chlorophenyl)ethanol + NAD+
-
low activity
-
-
r
2-chlorocyclohexanone + NADH + H+
? + NAD+
3% activity compared to cyclohexanone
-
-
?
2-decalone + NADH + H+
? + NAD+
28% activity compared to cyclohexanone
-
-
?
2-decanol + NAD+
2-decanone + NADH + H+
weak activity
-
-
r
2-ethylhexan-1-ol + NAD+
2-ethylhexanal + NADH
Sporotrichum pulverulentum
-
weak activity
-
-
?
2-heptanol + NAD+
heptan-2-one + NADH + H+
62% of the activity with 1-phenylethanol
-
-
?
2-heptanone + NADH
(S)-2-heptanol + NAD+ + H+
-
-
79% enantiomeric excess
-
?
2-heptanone + NADH + H+
(R)-2-heptanol + NAD+
-
229% of the activity with phenyl trifluoromethyl ketone
99% enantiomeric excess
-
?
2-hexanone + NADH + H+
?
-
activity is 1.6fold higher than with N-benzyl-3-pyrrolidinone
-
-
?
2-hexanone + NADH + H+
hexan-2-ol + NAD+
-
50.4fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
2-hydroxyacetophenone + NADPH + H+
(S)-1-phenyl-1,2-ethanediol + NADP+
-
-
-
?
2-methoxybenzaldehyde + NADH + H+
2-methoxybenzylalcohol + NAD+
-
13% of the activity with 2,2,2-trifluoroacetophenone
-
-
?
2-methoxybenzyl alcohol + NAD+
2-methoxybenzaldehyde + NADH + H+
-
25% of the activity with (S)-(-)-1-phenylethanol
-
-
?
2-methyl-2,4-pentanediol + NAD+
?
1% activity compared to cyclohexanol
-
-
?
2-methylbutyraldehyde + NADH + H+
2-methylbutanol + NAD+
-
1.4% of the activity with acetaldehyde
-
-
?
2-methylcyclohexanone + NADH + H+
2-methylcyclohexanol + NAD+
13% of the activity compared to 1-phenyl-1,2-propanedione
-
-
?
2-methylcyclohexanone + NADH + H+
? + NAD+
46% activity compared to cyclohexanone
-
-
?
2-methylpropionaldehyde + NADH + H+
2-methylpropanal + NAD+
-
3.3% of the activity with acetaldehyde
-
-
?
2-nitrobenzaldehyde + NADH + H+
(2-nitrophenyl)methanol + NAD+
-
33% of activity with N-benzyl-3-pyrrolidinone
-
-
?
2-nitrobenzaldehyde + NADH + H+
2-nitrobenzyl alcohol + NAD+
-
low activity
-
-
r
2-nonanol + NAD+
2-nonanone + NADH + H+
weak activity
-
-
r
2-octanone + NADPH + H+
octan-2-ol + NADP+
11.9% of the activity with 2-hydroxyacetophenone and NADPH
-
-
?
2-oxo-4-methylpentane + NADH
4-methylpentan-2-ol + NAD+
-
-
-
-
?
2-oxo-butyric acid + NADH + H+
2-hydroxybutyric acid + NAD+
-
15% of activity with N-benzyl-3-pyrrolidinone
-
-
?
2-oxopropanal + NADH + H+
? + NAD+
328% of the activity with acetoin
-
-
r
2-pentanone + NADH
(S)-2-pentanol + NAD+ + H+
-
-
60% enantiomeric excess
-
?
2-pentanone + NADPH + H+
pentan-2-ol + NADP+
11.9% of the activity with 2-hydroxyacetophenone and NADPH
-
-
?
2-phenylcyclohexanone + NADH + H+
? + NAD+
2% activity compared to cyclohexanone
-
-
?
2-phenylethanol + NAD+
2-phenylethanone + NADH + H+
57% activity compared to cyclohexanol
-
-
r
2-phenylpropanal + NADH + H+
(S)-2-phenylpropanol + NAD+
-
18 h, 74% yield, 98% enantiomeric excess
-
-
?
2-propanol + NAD+
aceton + NADH + H+
-
-
irreversible, no measurable activity with acetone
-
ir
2-[3-(2-phenyl-1,3-dioxolan-2-yl)phenyl]propanal + NADH + H+
(S)-2-(3-(2-phenyl-1,3-dioxolan-2-yl)phenyl)propanol + NAD+
-
18 h, 95% yield, 61% enantiomeric excess
-
-
?
3',4'-dimethoxyphenylacetone + NADH + H+
1-(3,4-dimethoxyphenyl)propan-2-ol + NAD+
-
24% of the activity with phenyl trifluoromethyl ketone
-
-
?
3'-bromoacetophenone + NADH + H+
1-(3-bromophenyl)ethanol + NAD+
-
151% of the activity with phenyl trifluoromethyl ketone
-
-
?
3'-chloroacetophenone + NADH + H+
1-(3-chlorophenyl)ethanol + NAD+
-
70% of the activity with phenyl trifluoromethyl ketone
-
-
?
3'-methoxyacetophenone + NADH + H+
1-(3-methoxyphenyl)ethanol + NAD+
-
51% of the activity with phenyl trifluoromethyl ketone
-
-
?
3,3,5-trimethylcyclohexanone + NADH + H+
? + NAD+
2% activity compared to cyclohexanone
-
-
?
3,4-dimethylbenzyl alcohol + NAD+
3,4-dimethylbenzaldehyde + NADH + H+
45% activity compared to cyclohexanol
-
-
r
3,4-hexanedione + NADH + H+
?
-
77% of the activity with N-benzyl-3-pyrrolidinone
-
-
?
3,4-methylenedioxyphenyl acetone + NADH
(S)-(3,4-methylenedioxyphenyl)-2-propanol + NAD+ + H+
-
-
-
-
-
3,5-dimethylcyclohexanol + NAD+
3,5-dimethylcyclohexanone + NADH + H+
1% activity compared to cyclohexanol
-
-
r
3-acetylpyridine + NADH + H+
1-pyridin-3-ylethanol + NAD+
-
7.9fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
3-aminobenzyl alcohol + NAD+
3-aminobenzaldehyde + NADH + H+
8% activity compared to cyclohexanol
-
-
r
3-bromobenzyl alcohol + NAD+
3-bromobenzaldehyde + NADH + H+
-
-
-
-
?
3-bromobenzylalcohol + NAD+
3-bromobenzaldehyde + NADH + H+
-
-
-
-
?
3-chloro-2-butanone + NADH + H+
3-chlorobutan-2-ol + NAD+
-
151% of the activity with phenyl trifluoromethyl ketone
-
-
?
3-heptanol + NAD+
3-heptanone + NADH + H+
-
93% of the activity with 2-propanol
-
-
r
3-methoxy-1-phenylpropan-1-one + NADH
3-methoxy-1-phenylpropan-1-ol + NAD+
-
-
-
-
?
3-methoxybenzaldehyde + NADH + H+
3-methoxybenzyl alcohol + NAD+
-
-
-
-
r
3-methoxybenzaldehyde + NADH + H+
3-methoxybenzylalcohol + NAD+
-
14% of the activity with 2,2,2-trifluoroacetophenone
-
-
?
3-methoxybenzylalcohol + NAD+
3-methoxybenzaldehyde + NADH + H+
-
-
-
-
?
3-methyl-2-cyclohexenone + NADH + H+
? + NAD+
1% activity compared to cyclohexanone
-
-
?
3-methylbutan-2-ol + NAD+
3-methylbutan-2-one + NADH
-
R-(-)-3-methylbutan-2-ol and S-(+)-3-methylbutan-2-ol
-
-
?
3-methylbutanol + NAD+
3-methylbutanone + NADH + H+
133% activity compared to cyclohexanol
-
-
r
3-methylbutyraldehyde + NADH + H+
3-methylbutanol + NAD+
-
2.9% of the activity with acetaldehyde
-
-
?
3-methylcyclohexanol + NAD+
3-methylcyclohexanone + NADH + H+
14% of activity compared to (S)-1-indanol
-
-
?
3-methylcyclohexanol + NAD+
?
10% of the activity compared to isoborneol
-
-
?
3-methylcyclohexanone + NADH + H+
3-methylcyclohexanol + NAD+
33% of the activity compared to 1-phenyl-1,2-propanedione
-
-
?
3-methylphenylethyl alcohol + NAD+
?
64% activity compared to cyclohexanol
-
-
?
3-pentanone + NADPH + H+
pentan-3-ol + NADP+
7.1% of the activity with 2-hydroxyacetophenone and NADPH
-
-
?
3-penten-2-one + NADH + H+
? + NAD+
2% activity compared to cyclohexanone
-
-
?
3-phenylpropanol + NAD+
3-phenylpropanal + NADH + H+
-
135% of the activity with 2-phenylethanol
-
-
?
3-phenylpropionaldehyde + NADH
3-phenylpropan-1-ol + NAD+
-
1218% of the activity with phenyl trifluoromethyl ketone
-
-
?
3-phenylpropionaldehyde + NADH + H+
3-phenylpropanol + NAD+
-
6.9fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
3beta,17beta-dihydroxy-5beta-androstane + NAD+
5beta-androstan-3,17dione + NADH
-
-
-
-
?
3beta,7alpha,12alpha-trihydroxy-5beta-cholanoic acid + NAD+
? + NADH
-
-
-
-
?
3beta-hxdroxy-5alpha-cholanoate + NAD+
3-oxo-5alpha-cholanoate + NADH
-
-
-
-
?
4'-bromoacetophenone + NADH + H+
1-(4-bromophenyl)ethanol + NAD+
-
77% of the activity with phenyl trifluoromethyl ketone
-
-
?
4'-chloroacetophenone + NADH + H+
1-(4-chlorophenyl)ethanol + NAD+
-
60% of the activity with phenyl trifluoromethyl ketone
-
-
?
4'-chlorobutyrophenone + NADH + H+
1-(4-chlorophenyl)butan-1-ol + NAD+
-
10% of the activity with 2,2,2-trifluoroacetophenone
-
-
?
4-acetylpyridine + NADH + H+
1-pyridin-4-ylethanol + NAD+
-
64.5fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
4-bromobenzyl alcohol + NAD+
4-bromobenzaldehyde + NADH + H+
-
-
-
-
?
4-bromobenzylalcohol + NAD+
4-bromobenzaldehyde + NADH + H+
-
-
-
-
?
4-carboxybenzaldehyde + NADH + H+
4-carboxybenzyl alcohol + NAD+
-
-
-
-
?
4-carboxybenzaldehyde + NADH + H+
4-carboxybenzylalcohol + NAD+
-
-
-
-
?
4-ethylcyclohexanol + NAD+
4-ethylcyclohexanone + NADH + H+
60% activity compared to cyclohexanol
-
-
r
4-ethylcyclohexanone + NADH + H+
? + NAD+
22% activity compared to cyclohexanone
-
-
?
4-hydroxy-2-butanone + NADH + H+
2,4-dihydroxybutane + NAD+
-
26% of the activity with phenyl trifluoromethyl ketone
-
-
?
4-hydroxynonenal + NADH + H+
4-hydroxynonenol + NAD+
-
substrate of isozyme ADH4
-
-
r
4-methoxy-1-naphthaldehyde + NAD+
4-methoxy-1-naphthol + NADH + H+
-
fluorogenic substrate of class I and II isozymes
-
-
?
4-methoxy-1-naphthaldehyde + NAD+
4-methoxy-1-naphthyl alcohol + NADH + H+
-
substrate for class I ADH
-
-
?
4-methoxy-1-naphthaldehyde + NADH + H+
4-methoxynaphthalene-1-carbaldehyde + NAD+
-
substrate for class I ADH
-
-
r
4-methoxybenzaldehyde + NADH + H+
4-methoxybenzyl alcohol + NAD+
-
-
51% of the activity with butan-2-ol
-
?
4-methoxybenzaldehyde + NADH + H+
4-methoxybenzylalcohol + NAD+
-
13% of the activity with 2,2,2-trifluoroacetophenone
-
-
?
4-methoxybenzylalcohol + NAD+
4-methoxybenzaldehyde + NADH + H+
-
-
-
-
r
4-methoxyphenylacetone + NADH
(2S)-1-(4-methoxyphenyl)propan-2-ol + NAD+ + H+
-
-
-
-
?
4-methylcyclohexanol + NAD+
4-methylcyclohexanone + NADH + H+
56% activity compared to cyclohexanol
-
-
r
4-methylcyclohexanone + NADH + H+
4-methylcyclohexanol + NAD+
60% of the activity compared to 1-phenyl-1,2-propanedione
-
-
?
4-methylcyclohexanone + NADH + H+
? + NAD+
25% activity compared to cyclohexanone
-
-
?
4-nitrobenzaldehyde + NADH + H+
4-nitrobenzylalcohol + NAD+
-
-
-
-
?
4-nitrobenzyl alcohol + NAD+
4-nitrobenzaldehyde + NADH + H+
94% activity compared to benzyl alcohol
-
-
?
4-nitrosodimethylaniline + NAD+
? + NADH + H+
-
photometric assay substrate
-
-
?
4-phenylbutan-2-one + NADH
4-phenylbutan-2-ol + NAD+
-
-
-
-
?
5-acetyl-7-chlorofuro[2,3-c]pyridine + NADH + H+
5-(1-hydroxyethyl)-7-chlorofuro[2,3-c]pyridine + NAD+
-
-
-
-
r
5-acetylfuro[2,3-c]pyridine + NADH + H+
5-(1-hydroxyethyl)furo[2,3-c]pyridine + NAD+
-
-
-
-
r
5-hydroxymethylfurfural + NADH + H+
(furan-2,5-diyl)dimethanol + NAD+
mutant enzyme S109P/L116S/Y294C
-
-
?
5alpha-androstan-17beta-ol-3-one + NADH + H+
3beta,17beta-dihydroxy-5alpha-androstan + NAD+
5alpha-pregnan-3beta-ol-20-one + NAD+
5alpha-pregnan-3,20-dione + NADH
-
low activity
-
-
?
5beta-cholanic acid-3-one + NADH
5beta-cholanic acid-3-ol + NAD+
-
low activity
-
-
?
5beta-pregnan-21-ol-3,20-dione hemisuccinate + NADH
5beta-pregnan-3,20,21-trione hemisuccinate + NADH
-
-
-
-
?
6-benzyloxy-3,5-dioxo-hexanoic acid ethyl ester + NADH + H+
(3R,5S)-6-benzyloxy-3,5-dihydroxy-hexanoic acid ethyl ester + NAD+
-
-
-
-
-
6-methoxy-2-naphthaldehyde + NADH + H+
(6-methoxynaphthalen-2-yl)methanol + NAD+
-
substrate for class II ADH
-
-
r
6-methoxy-2-naphthaldehyde + NADH + H+
6-methoxy-2-naphthyl alcohol + NAD+
-
substrate for class II ADH
-
-
?
6-methoxy-2-naphthaldehyde + NADH + H+
6-methoxy-2-naphtol + NAD+
-
class II isozyme, reductive activity
-
-
?
a primary alcohol + NAD+
an aldehyde + NADH + H+
-
ADH3 is involved in multiple cellular pathways, as diverse as formaldehyde detoxification, retinoid metabolism and NO homeostasis, ADH3 is considered to play only a minor role in hepatic alcohol metabolism because ethanol concentrations rarely exceed 50 mM
-
-
?
acetoin + NAD+
diacetyl + NADH
18% of the activity with 2,3-butanediol
-
-
?
acetone + NAD+ + H2O
? + NADH + H+
about 5% of the activity with 1-octanol
-
-
r
acetone + NADH + H+
propan-2-ol + NAD+
-
1.9fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
acetone + NADPH + H+
propan-2-ol + NADP+
14.7% of the activity with 2-hydroxyacetophenone and NADPH
-
-
?
acetophenone + NADH
(R)-alpha-phenyl ethanol + NAD+
-
the enzyme exhibits high stereoselectivity in the desymmetrization of the prochiral ketone acetophenone, producing optically pure (R)-alpha-phenyl ethanol at high conversion
-
-
?
acetophenone + NADH + H+
(R)-1-phenylethanol + NAD+
-
6% of the activity with phenyl trifluoromethyl ketone, in the reverse reaction 87% of the activity with 2-propanol
99% enantiomeric excess
-
?
acetophenone + NADH + H+
(S)-(-)-1-phenylethanol + NAD+
-
more than 99% enantiomeric excess
-
-
r
acetophenone + NADH + H+
(S)-1-phenylethanol + NAD+
-
-
99% enantiomeric excess
-
r
acetylacetone + NADH + H+
?
-
63% of the activity with N-benzyl-3-pyrrolidinone
-
-
?
acetylacetone + NADH + H+
acetophenone + NADH + H+
1% activity compared to cyclohexanone
1% activity compared to cyclohexanone
-
r
alpha-ethyl benzoylformate + NADH + H+
ethyl (R)-()-mandelate + NAD+
-
-
95% enantiomeric excess
-
r
alpha-methyl benzoylformate + NADH + H+
methyl (R)-mandelate + NAD+
-
-
92% enantiomeric excess
-
r
benzil + NADH + H+
(R)-benzoin + NAD+
62% of the activity compared to 1-phenyl-1,2-propanedione. The enzyme catalyses the asymmetric reduction of benzil to (R)-benzoin with both excellent conversion (98%) and optical purity (98%) by way of an efficient in situ NADH-recycling system involving a second thermophilic ADH
-
-
?
benzoin + NADH + H+
1,2-diphenylethane-1,2-diol
-
13% of activity with N-benzyl-3-pyrrolidinone
-
-
?
benzoylformic acid + NADPH + H+
mandelate + NADP+
2.4% of the activity with 2-hydroxyacetophenone and NADPH
-
-
?
benzyloxycarbonyl-3-pyrrolidinone + NADH + H+
(S)-benzyloxycarbonyl-3-pyrrolidinol + NAD+
-
production with 99.6% enantiomeric excess
-
-
?
butan-2-ol+ NAD+
butanone + NADH + H+
-
-
83% of the activity with butan-2-ol
-
?
butanal + NADH
1-butanol + NAD+ + H+
-
% of the activity with phenyl trifluoromethyl ketone
-
-
ir
butyraldehyde + NADH + H+
butanol + NAD+
-
56% of the activity with acetaldehyde
-
-
?
butyraldehyde + NADPH + H+
butanol + NADP+
-
22% of the activity with NADH
-
-
?
choline + NAD+
? + NADH + H+
3% activity compared to benzyl alcohol
-
-
?
cis-4-methylcyclohexanol + NAD+
4-methylcyclohexanone + NADH
-
-
-
-
?
cis-decahydro-1-naphthol + NAD+
?
11% of activity compared to (S)-1-indanol
-
-
?
cyclohexanone + NADH + H+
?
-
activity is 2.1fold higher than with N-benzyl-3-pyrrolidinone
-
-
?
cyclopentanone + NADH + H+
? + NAD+
1% activity compared to cyclohexanone
-
-
?
D-arabinose + NADH + H+
D-arabitol + NAD+
66% of the activity with 2,3-butanediol
-
-
?
decyl aldehyde + NADH + H+
1-decanol + NAD+
21% activity compared to benzyl alcohol
-
-
?
diacetyl + NADH + H+
acetoin + NAD+
150% of the activity with acetoin
-
-
?
dihydro-4,4-dimethyl-2,3-furandione + NADH + H+
?
-
13.1fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
dihydroxyacetone + NADH + H+
glycerol + NAD+
36% of the activity with acetoin
-
-
?
dihydroxyacetone phosphate + NADH + H+
glycerol phosphate + NAD+
82% of the activity with acetoin
-
-
?
DL-glyceraldehyde + H+
glycerol + NAD+
31% of the activity with acetoin
-
-
?
docosanol + NAD+
? + NADH + H+
-
immobilized HLAD shows about 60% reaction rate and free HLAD shows about 20% reaction rate with docosanol compared to ethanol at pH 8.8 and 30°C
-
-
?
dodecanol + NAD+
dodecanal + NADH + H+
-
immobilized HLAD shows about 60% reaction rate and free HLAD shows about 35% reaction rate with dodecanol compared to ethanol at pH 8.8 and 30°C
-
-
?
ethanol + 2 NADP+ + H2O
acetic acid + 2 NADPH + 2 H+
-
-
-
r
ethanol + 3-benzoylpyridine-adenine dinucleotide
acetaldehyde + ?
-
rapid equilibrium bi bi mechanism
-
-
-
ethanol + NAD+
aldehyde + NADH + H+
-
immobilized HLAD shows 100% reaction rate and free HLAD shows about 55% reaction rate with ethanol at pH 8.8 and 30°C
-
-
?
ethyl 2-oxopropanoate + NADPH + H+
(R)-ethyl 2-hydroxypropanoate + NADP+
294& of the activity with acetoin
-
-
r
ethyl 3-methyl-2-oxobutyrate + NADH + H+
?
1-phenyl-1,2-propanedione and ethyl 3-methyl-2-oxobutyrate are the best substrate in the reduction reaction
-
-
?
ethyl 3-methyl-2-oxobutyrate + NADH + H+
ethyl-2-hydroxy-3-methylbutyrate + NAD+
-
33% of the activity with phenyl trifluoromethyl ketone
-
-
?
ethyl 3-oxobutanoate + NADH
ethyl 3-hydroxybutanoate + NAD+
-
-
-
-
?
ethyl 3-oxobutanoate + NADH + H+
ethyl 3-hydroxybutanoate + NAD+
-
309% of the activity with phenyl trifluoromethyl ketone
-
-
?
ethyl 3-oxobutyrate + NADH + H+
ethyl (S)-3-hydroxybutyrate + NAD+
-
-
-
-
-
ethyl 3-oxohexanoate + NADH
ethyl 3-hydroxyhexanoate + NAD+
-
-
-
-
?
ethyl 3-oxopentanoate + NADH
ethyl 3-hydroxypentanoate + NAD+
-
-
-
-
?
ethyl 3-phenyl-3-oxopropanoate + NADH
ethyl 3-phenyl-3-hydroxypropanoate + NAD+
-
-
-
-
?
ethyl 4-bromo-3-oxobutanoate + NADH + H+
ethyl 4-bromo-3-hydroxybutanoate
-
511% of the activity with phenyl trifluoromethyl ketone
-
-
?
ethyl 4-chloro-3-oxobutanoate + NADH + H+
ethyl 4-chloro-3-hydroxybutanoate + NAD+
-
809% of the activity with phenyl trifluoromethyl ketone
-
-
?
ethyl 4-chloroacetoacetate + NADH + H+
?
-
6.8fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
ethyl 4-chloroacetoacetate + NADH + H+
ethyl 4-chloro-3-hydroxybutanoate + NAD+
-
-
-
-
r
ethyl 4-chloroacetoacetate + NADPH
?
activity is 1.48fold higher than with 2-hydroxyacetophenone and NADPH
-
-
?
ethyl acetoacetate + NADH + H+
?
-
42.4fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
ethyl benzoylformate + NADH
?
about 30% of the activity compared to isatin
-
-
?
ethyl benzoylformate + NADH
ethyl (R)-mandelate + NAD+
-
enantiomeric excess of 99.9%
-
-
?
ethyl benzoylformate + NADH + H+
?
23% of the activity compared to 1-phenyl-1,2-propanedione
-
-
?
ethyl benzoylformate + NADH + H+
ethyl (R)-(-)-mandelate + NAD+
-
95% enantiomeric excess
-
-
?
ethyl oxo(phenyl)acetate + NADH + H+
ethyl hydroxy(phenyl)acetate + NAD+
-
100% of the activity with 2,2,2-trifluoroacetophenone
-
-
r
ethyl pyruvate + NADH
ethyl 2-hydroxypropanoate + NAD+
-
-
-
-
?
ethyl pyruvate + NADH + H+
ethyl 2-hydroxypropanoate + NAD+
-
488% of the activity with phenyl trifluoromethyl ketone
-
-
?
ethyl pyruvate + NADH + H+
ethyl 2-hydroxypropionate + NAD+
16% of the activity compared to 1-phenyl-1,2-propanedione
-
-
?
ethyl trifluoroacetoacetate + NADPH + H+
1-ethoxy-2,2,2-trifluoroethanol + NADP+
4.3% of the activity with 2-hydroxyacetophenone and NADPH
-
-
?
furfural + NADH
furfuryl alcohol + NADH
-
activity with enzyme form ADH I, no activity with enzyme form ADH II
-
r
furfural + NADH + H+
furfuryl alcohol + NADH
mutant enzyme S109P/L116S/Y294C
-
-
?
glutaraldehyde + NADH + H+
?
-
70.8fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
glycerol + 2 NAD+ + H2O
? + 2 NADH + 2 H+
about 45% of the activity with ethanol
-
-
r
heptaldehyde + NADH + H+
? + NAD+
33% activity compared to benzyl alcohol
-
-
?
hexadecanol + NAD+
hexadecanal + NADH + H+
-
immobilized HLAD shows about 60% reaction rate and free HLAD shows about 15% reaction rate with hexadecanol compared to ethanol at pH 8.8 and 30°C
-
-
?
hexaldehyde + NADH + H+
1-hexanol + NAD+
7% activity compared to benzyl alcohol
-
-
?
hexanal + NADH + H+
1-hexanone + NAD+
-
49% of the activity with acetaldehyde
-
-
?
hexanal + NADH + H+
hexan-1-ol + NAD+
16% of the activity with acetoin
-
-
?
hexanal + NADH + H+
n-hexanol + NAD+
-
22.3fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
hydrocinnamaldehyde + NADH + H+
hydrocinnamyl alcohol + NAD+
12% activity compared to benzyl alcohol
-
-
r
hydrocinnamyl alcohol + NAD+
hydrocinnamaldehyde + NADH + H+
31% activity compared to benzyl alcohol
-
-
r
hydroxyacetone + NADH + H+
propane-1,2-diol + NAD+
-
27% of the activity with N-benzyl-3-pyrrolidinone
-
-
?
isoamylalcohol + 2 NAD+ + H2O
? + 2 NADH + 2 H+
about 5% of the activity with 1-octanol
-
-
r
isoborneol + NAD+
?
isoborneol is the best substrate in the oxidation reaction
-
-
?
levulinic acid + NADH + H+
?
-
11% of activity with N-benzyl-3-pyrrolidinone
-
-
?
m-chlorophenacyl chloride + NADH + H+
2-chloro-1-(3-chlorophenyl)ethanol + NAD+
-
4.6fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
m-nitrobenzaldehyde + NAD+
m-nitrobenzyl alcohol + NADH + H+
-
substrate of class IV ADH
-
-
?
methanol + 2 NAD+ + H2o
formic acid + 2 NADH + 2 H+
about 25% of the activity with 1-octanol
-
-
r
methyl 3-oxobutanoate + NADH + H+
methyl 3-hydroxybutanoate + NAD+
-
130% of the activity with phenyl trifluoromethyl ketone
-
-
?
methyl 4-bromo-3-oxobutanoate + NADH + H+
methyl 4-bromo-3-hydroxybutanoate + NAD+
-
164% of the activity with phenyl trifluoromethyl ketone
-
-
?
methyl benzoylformate + NADH + H+
methyl (R)-(-)-mandelate + NAD+
-
92% enantiomeric excess
-
-
?
methyl benzoylformate + NADH + H+
methyl (S)-mandelate + NAD+
-
6 h, 100% conversion, 17% enantiomeric excess
-
r
methyl glyoxal + NADH + H+
?
-
3.5fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
methyl o-chlorobenzoylformate + NADH
?
about 55% of the activity compared to isatin
-
-
?
methyl o-chlorobenzoylformate + NADH + H+
methyl (R)-o-chloromandelate + NAD+
-
6 h, 99% conversion, 72% enantiomeric excess
-
r
methyl oxo(phenyl)acetate + NADH + H+
methyl hydroxy(phenyl)acetate + NAD+
-
57% of the activity with 2,2,2-trifluoroacetophenone
-
-
r
methyl pyruvate + NADH + H+
methyl 2-hydroxypropanoate + NAD+
-
18.9fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
methylbenzoylformate + NADH + H+
?
-
13% of the activity with 2,2,2-trifluoroacetophenone
-
-
?
methylglyoxal + NADH
? + NADH
-
11.9% of the activity with acetaldehyde
-
-
?
N-benzyl-3-piperidone + NADH + H+
N-benzylpiperidin-3-ol + NAD+
-
2.3fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
N-benzyl-3-pyrrolidinol + NAD+
1-benzylpyrrolidin-3-one + NADH + H+
-
33% of the activity with (S)-N-benzyl-3-pyrrolidinol
-
-
?
N-benzyl-3-pyrrolidinone + NADH + H+
(R)-N-benzyl-3-pyrrolidinol + NAD+
-
(R)-stereoselectivity of the reduction carried out with the heat-treated cells
-
-
r
N-benzyl-4-piperidone + NADH + H+
N-benzylpiperidin-4-ol + NAD+
-
10.7fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
n-butylaldehyde + NADH + H+
butanal + NAD+
-
activity is 1.8fold higher than with N-benzyl-3-pyrrolidinone
-
-
?
n-butyraldehyde + NADH + H+
n-butanol + NAD+
-
7.3fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
n-hexylaldehyde + NADH + H+
hexanal + NAD+
-
activity is 1.6fold higher than with N-benzyl-3-pyrrolidinone
-
-
?
n-octylaldehyde + NADH + H+
n-octanol + NAD+
-
activity is 1.7fold higher than with N-benzyl-3-pyrrolidinone
-
-
?
N-tert-butoxycarbonyl-3-pyrrolidinone + NADH + H+
(S)-N-tert-butoxycarbonyl-3-pyrrolidinol + NAD+
-
production of (S)-N-tert-butoxycarbonyl-3-pyrrolidinol with 99.6% enantiomeric excess
-
-
?
n-valeraldehyde + NADH + H+
n-pentanol + NAD+
-
activity is 2.8fold higher than with N-benzyl-3-pyrrolidinone
-
-
?
nonyl aldehyde + NADH + H+
1-nonanol + NAD+
25% activity compared to benzyl alcohol
-
-
?
nonylphenol polyethoxylate 9 + NAD+
? + NADH
7% activity compared to benzyl alcohol
-
-
?
octanoic acid + 2 NADH + 2 H+
1-octanol + 2 NAD+ + H2o
-
-
-
r
octyl aldehyde + NADH + H+
1-octanol + NAD+
29% activity compared to benzyl alcohol
-
-
?
octylphenol polyethoxylate 2 + NAD+
? + NADH
59% activity compared to benzyl alcohol
-
-
?
octylphenol polyethoxylate 8 + NAD+
? + NADH
7% activity compared to benzyl alcohol
-
-
?
oxalacetic acid + NADH + H+
?
-
14% of activity with N-benzyl-3-pyrrolidinone
-
-
?
p-chlorobenzaldehyde + NADH + H+
p-chlorobenzyl alcohol + NAD+
-
1.2fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
p-nitrobenzaldehyde + NADH + H+
p-nitrobenzyl alcohol + NAD+
-
substrate of isozyme ADH4
-
-
r
p-nitrobenzyloxycarbonyl-3-pyrrolidinone + NADH + H+
(S)-N-p-nitrobenzyloxycarbonyl-3-pyrrolidinol + NAD+
-
production with 90.7% enantiomeric excess
-
-
?
p-nitrophenyl octanoate + H2O
p-nitrophenol + octanoate
-
acid-assisted nucleophilic catalysis involving the ammonium ion of Lys and the thiolate of Cys in the acyl-oxygen cleavage
-
?
pentan-1-ol + NAD+
pentanal + NADH + H+
-
-
76% of the activity with butan-2-ol
-
?
pentanal + NADH
1-pentanol + NAD+ + H+
-
132% of the activity with phenyl trifluoromethyl ketone, in the reverse reaction 5% of the activity with 2-propanol
-
-
?
pentanol + NAD+
1-pentanal + NADH + H+
about 10% of the activity with ethanol or 1-propanol
-
-
?
pentanol + NAD+
valeraldehyde + NADH + H+
-
240% activity compared to cyclohexanone
-
r
phenyl trifluoromethyl ketone + NADH + H+
(S)-1-phenyltrifluoroethanol + NAD+
-
-
more than 99% enantiomeric excess
-
?
phenylethanol + NAD+
phenylacetaldehyde + NADH
-
R-(+)-phenylethanol and S-(-)-phenylethanol
-
-
?
phenylethanol + NAD+
phenylacetaldehyde + NADH + H+
-
15% of activity with N-benzyl-3-pyrrolidinol
-
-
?
phenylglyoxylic acid + NADH + H+
hydroxy(phenyl)acetic acid + NAD+
-
enzyme covalently immobilized to magnetic Fe3O4 nanoparticles via glutaraldehyde retains 48.77% activity of its original activity
-
-
?
polyoxyethylene 8 decyl ether + NAD+
? + NADH
12% activity compared to benzyl alcohol
-
-
?
prop-2-en-1-ol+ NAD+
prop-2-enal + NADH + H+
-
-
85% of the activity with butan-2-ol
-
?
propan-1-ol+ NAD+
propanal + NADH + H+
-
-
68% of the activity with butan-2-ol
-
r
propan-2-ol+ NAD+
acetone + NADH + H+
-
-
79% of the activity with butan-2-ol
-
?
propanal + NADH + H+
propan-1-ol + NAD+
-
-
38% of the activity with butan-2-ol
-
r
propionaldehyde + NADH + H+
?
-
activity is 1.1fold higher than with N-benzyl-3-pyrrolidinone
-
-
?
propiophenone + NADH + H+
1-phenylpropan-1-ol + NAD+
-
27% of activity with N-benzyl-3-pyrrolidinone
-
-
?
pyridine-3-aldehyde + NADH + H+
pyridin-3-yl ethanol + NAD+
-
82% of activity with N-benzyl-3-pyrrolidinone
-
-
?
pyridine-4-aldehyde + NADH + H+
pyridin-4-yl methanol + NAD+
-
4.4fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
pyruvaldehyde + NADH + H+
lactaldehyde + NAD+
81% of the activity with acetoin
-
-
?
R-(+)-trans-bicyclo(2.2.1)-heptanol + NAD+
R-(+)-trans-bicyclo(2.2.1)-heptanal + NADH
-
R-(+)-trans-bicyclo(2.2.1)-heptanol and S-(-)-trans-bicyclo(2.2.1)-heptanol
-
-
?
rac-3-methylcyclohexanone + NADH + H+
(1S,3S)-3-methylcyclohexanol + NAD+
-
-
-
-
?
S-(-)-cis-bicyclo(2.2.1)-heptanol + NAD+
S-(-)-cis-bicyclo(2.2.1)-heptanal + NADH
-
-
-
-
?
tert-butyl 3-oxobutanoate + NADH + H+
tert butyl 3-hydroxybutanoate + NAD+
-
568% of the activity with phenyl trifluoromethyl ketone
-
-
?
tetracosanol + NAD+
? + NADH + H+
-
immobilized HLAD shows about 55% reaction rate and free HLAD shows about 15% reaction rate with tetracosanol compared to ethanol at pH 8.8 and 30°C
-
-
?
tetrahydro-4H-pyran-4-one + NADH + H+
? + NAD+
10% activity compared to cyclohexanone
-
-
?
tetralin-1-ol + NAD+
3,4-dihydronaphthalen-1(2H)-one + NADH + H+
51% of the activity compared to isoborneol
-
-
?
trans-4-(N,N-dimethylamino)-cinnamaldehyde + NADH
trans-4-(N,N-dimethylamino)-cinnamyl alcohol + NAD+
-
-
-
-
?
trans-4-methylcyclohexanol + NAD+
4-methylcyclohexanone + NADH
-
-
-
-
?
trans-cinnamyl alcohol + NAD+
(2E)-3-phenylprop-2-enal + NADH + H+
-
activity is 3.9fold higher than with (S)-(-)-1-phenylethanol
-
-
?
Triton X-100 + NAD+
? + NADH
7% activity compared to benzyl alcohol
-
-
?
Triton X-114 + NAD+
? + NADH
3% activity compared to benzyl alcohol
-
-
?
Triton X-165 + NAD+
? + NADH
24% activity compared to benzyl alcohol
-
-
?
Triton X-35 + NAD+
? + NADH
43% activity compared to benzyl alcohol
-
-
?
Triton X-405 + NAD+
? + NADH
19% activity compared to benzyl alcohol
-
-
?
Triton X-45 + NAD+
? + NADH
7% activity compared to benzyl alcohol
-
-
?
(2E)-2-methylpent-2-enal + NADPH + H+
(2E)-2-methylpent-2-en-1-ol + NADP+
41.5% of the activity with (2E)-but-2-enal, yield 95% after 12 h
-
-
?
(2E)-2-methylpent-2-enal + NADPH + H+
(2E)-2-methylpent-2-en-1-ol + NADP+
41.5% of the activity with (2E)-but-2-enal, yield 95% after 12 h
-
-
?
(2E)-3,7-dimethylocta-2,6-dienal + NADPH + H+
(2E)-3,7-dimethylocta-2,6-dien-1-ol + NADP+
37.4% of the activity with (2E)-but-2-enal, yield 87% after 12 h
-
-
?
(2E)-3,7-dimethylocta-2,6-dienal + NADPH + H+
(2E)-3,7-dimethylocta-2,6-dien-1-ol + NADP+
37.4% of the activity with (2E)-but-2-enal, yield 87% after 12 h
-
-
?
(E)-hex-2-en-1-ol + NAD+
(E)-hex-2-en-1-one + NADH
-
43.2% of the activity with ethanol
-
-
?
(R)-2-butanol + NAD+
2-butanone + NADH + H+
-
55% of activity with N-benzyl-3-pyrrolidinol
-
-
?
(R)-2-butanol + NAD+
2-butanone + NADH + H+
-
55% of activity with N-benzyl-3-pyrrolidinol
-
-
?
(R)-2-butanol + NAD+
2-butanone + NADH + H+
-
50% of the activity with 2-propanol
-
-
ir
(R)-2-butanol + NAD+
2-butanone + NADH + H+
-
50% of the activity with 2-propanol
-
-
ir
(R)-2-heptanol + NAD+
2-heptanone + NADH + H+
-
2469% of the activity with 2-propanol
-
-
r
(R)-2-heptanol + NAD+
2-heptanone + NADH + H+
-
2469% of the activity with 2-propanol
-
-
r
(R)-2-hexanol + NAD+
2-hexanone + NADH + H+
-
1906% of the activity with 2-propanol
-
-
r
(R)-2-hexanol + NAD+
2-hexanone + NADH + H+
-
1906% of the activity with 2-propanol
-
-
r
(R)-2-octanol + NAD+
2-octanone + NADH + H+
-
2406% of the activity with 2-propanol
-
-
r
(R)-2-octanol + NAD+
2-octanone + NADH + H+
-
2406% of the activity with 2-propanol
-
-
r
(R)-2-pentanol + NAD+
2-pentanone + NADH + H+
-
75% of the activity with 2-propanol
-
-
r
(R)-2-phenylpropanol + NAD+
(R)-2-phenylpropanal + NADH + H+
-
63% of the activity with 2-phenylethanol
-
-
?
(R)-2-phenylpropanol + NAD+
(R)-2-phenylpropanal + NADH + H+
-
63% of the activity with 2-phenylethanol
-
-
?
(R,S)-2-methylbutan-1-ol + NAD+
(R,S)-2-methyl-butan-1-one + NADH + H+
-
-
-
?
(R,S)-2-methylbutan-1-ol + NAD+
(R,S)-2-methyl-butan-1-one + NADH + H+
Saccharomyces carlsbergensis Y379-50
-
-
-
?
(R,S)-2-methylbutan-1-ol + NAD+
(R,S)-2-methyl-butan-1-one + NADH + H+
-
-
-
-
?
(S)-1-indanol + NAD+
1-indanone + NADH + H+
-
3900% of the activity with (S)-1-phenylethanol
-
-
r
(S)-2-butanol + NAD+
2-butanone + NADH + H+
-
275% of the activity with 2-propanol
-
-
ir
(S)-2-methylbutan-1-ol + NAD+
(S)-2-methyl-butanal + NADH + H+
-
-
-
?
(S)-2-methylbutan-1-ol + NAD+
(S)-2-methyl-butanal + NADH + H+
-
-
-
-
?
(S)-2-methylbutan-1-ol + NAD+
(S)-2-methyl-butanal + NADH + H+
-
-
-
-
-
(S)-2-octanol + NAD+
2-octanone + NADH + H+
-
81% of the activity with 2-propanol
-
-
r
(S)-2-pentanol + NAD+
2-pentanone + NADH + H+
-
25% of the activity with 2-propanol
-
-
r
(S)-alpha-tetralol + NAD+
alpha-tetralone + NADH + H+
-
-
-
r
(S)-alpha-tetralol + NAD+
alpha-tetralone + NADH + H+
-
-
-
r
(S)-alpha-tetralol + NAD+
alpha-tetralone + NADH + H+
-
2700% of the activity with (S)-1-phenylethanol
-
-
r
1,2-butanediol + NAD+
?
-
35% of the activity with (S)-N-benzyl-3-pyrrolidinol
-
-
?
1,3-propanediol + 2 NAD+ + H2O
? + 2 NADH + 2 H+
about 45% of the activity with ethanol
-
-
r
1,3-propanediol + 2 NAD+ + H2O
? + 2 NADH + 2 H+
about 5% of the activity with 1-octanol
-
-
r
1,3-propanediol + 2 NAD+ + H2O
? + 2 NADH + 2 H+
about 45% of the activity with ethanol
-
-
r
1,3-propanediol + 2 NAD+ + H2O
? + 2 NADH + 2 H+
about 5% of the activity with 1-octanol
-
-
r
1-(4-fluorophenyl)ethanol + NAD+
1-(4-fluorophenyl)ethanone + NADH + H+
119% of the activity with 1-phenylethanol
-
-
?
1-(4-fluorophenyl)ethanol + NAD+
1-(4-fluorophenyl)ethanone + NADH + H+
-
45% of the activity with (S)-(-)-1-phenylethanol
-
-
?
1-butanol + 2 NAD+ + H2O
butanoic acid + 2 NADH + 2 H+
about 45% of the activity with ethanol
-
-
r
1-butanol + 2 NAD+ + H2O
butanoic acid + 2 NADH + 2 H+
about 50% of the activity with 1-octanol
-
-
r
1-butanol + 2 NAD+ + H2O
butanoic acid + 2 NADH + 2 H+
about 45% of the activity with ethanol
-
-
r
1-butanol + 2 NAD+ + H2O
butanoic acid + 2 NADH + 2 H+
about 50% of the activity with 1-octanol
-
-
r
1-butanol + NAD+
butanal + NADH
-
111% of the activity with 2-phenylethanol
-
-
?
1-butanol + NAD+
butanal + NADH
-
111% of the activity with 2-phenylethanol
-
-
?
1-butanol + NAD+
butanal + NADH + H+
-
15.7% of the activity with ethanol
-
-
?
1-butanol + NAD+
butanal + NADH + H+
about 80% of activity with ethanol, ADH1
-
-
?
1-butanol + NAD+
butanal + NADH + H+
about 80% of activity with ethanol, ADH1
-
-
?
1-butanol + NAD+
butanal + NADH + H+
30% activity compared to benzyl alcohol
-
-
?
1-butanol + NAD+
butanal + NADH + H+
30% activity compared to benzyl alcohol
-
-
?
1-butanol + NAD+
butanal + NADH + H+
67.7% activity compared to ethanol
-
-
?
1-butanol + NAD+
butanal + NADH + H+
142% activity compared to cyclohexanol
-
-
r
1-butanol + NAD+
butanal + NADH + H+
142% activity compared to cyclohexanol
-
-
r
1-decanol + NAD+
decanal + NADH + H+
13% activity compared to benzyl alcohol
-
-
?
1-decanol + NAD+
decanal + NADH + H+
13% activity compared to benzyl alcohol
-
-
?
1-dodecanol + NAD+
dodecanal + NADH
-
68% of the activity with 2-phenylethanol
-
-
?
1-dodecanol + NAD+
dodecanal + NADH
-
68% of the activity with 2-phenylethanol
-
-
?
1-heptanol + NAD+
heptanal + NADH + H+
25% activity compared to benzyl alcohol
-
-
?
1-heptanol + NAD+
heptanal + NADH + H+
25% activity compared to benzyl alcohol
-
-
?
1-heptanol + NAD+
heptanal + NADH + H+
80% activity compared to cyclohexanol
-
-
r
1-heptanol + NAD+
heptanal + NADH + H+
80% activity compared to cyclohexanol
-
-
r
1-hexanol + 2 NAD+ + H2O
hexanoic acid + 2 NADH + 2 H+
about 55% of the activity with 1-octanol
-
-
r
1-hexanol + 2 NAD+ + H2O
hexanoic acid + 2 NADH + 2 H+
about 70% of the activity with ethanol
-
-
r
1-hexanol + 2 NAD+ + H2O
hexanoic acid + 2 NADH + 2 H+
about 70% of the activity with ethanol
-
-
r
1-hexanol + 2 NAD+ + H2O
hexanoic acid + 2 NADH + 2 H+
about 55% of the activity with 1-octanol
-
-
r
1-hexanol + NAD+
hexanal + NADH + H+
-
44% of the activity with 2-propanol, in the reverse reaction 1029% of the activity with phenyl trifluoromethyl ketone
-
-
r
1-hexanol + NAD+
hexanal + NADH + H+
about 90% of activity with ethanol, ADH1
-
-
?
1-hexanol + NAD+
hexanal + NADH + H+
about 90% of activity with ethanol, ADH1
-
-
?
1-hexanol + NAD+
hexanal + NADH + H+
61% activity compared to benzyl alcohol
-
-
?
1-hexanol + NAD+
hexanal + NADH + H+
61% activity compared to benzyl alcohol
-
-
?
1-hexanol + NAD+
hexanal + NADH + H+
15.3% activity compared to ethanol
-
-
?
1-hexanol + NAD+
hexanal + NADH + H+
109% activity compared to cyclohexanol
-
-
r
1-hexanol + NAD+
hexanal + NADH + H+
109% activity compared to cyclohexanol
-
-
r
1-indanol + NAD+
1-indanone + NADH + H+
26% of the activity compared to isoborneol
-
-
?
1-indanol + NAD+
1-indanone + NADH + H+
26% of the activity compared to isoborneol
-
-
?
1-indanol + NAD+
1-indanone + NADH + H+
-
1% activity compared to cyclohexanone
-
r
1-indanone + NADH + H+
(S)-1-indanol + NAD+
-
6 h, 50°C, 6% conversion, 25% enantiomeric excess
-
r
1-indanone + NADH + H+
(S)-1-indanol + NAD+
-
6 h, 50°C, 6% conversion, 25% enantiomeric excess
-
r
1-nonanol + NAD+
nonanal + NADH + H+
12% activity compared to benzyl alcohol
-
-
?
1-octanol + 2 NAD+ + H2O
octanoic acid + 2 NADH + 2 H+
best substrate
-
-
r
1-octanol + 2 NAD+ + H2O
octanoic acid + 2 NADH + 2 H+
about 30% of the activity with ethanol
-
-
r
1-octanol + 2 NAD+ + H2O
octanoic acid + 2 NADH + 2 H+
best substrate
-
-
r
1-octanol + NAD+
octanal + NADH
-
101% of the activity with 2-phenylethanol
-
-
?
1-octanol + NAD+
octanal + NADH
-
101% of the activity with 2-phenylethanol
-
-
?
1-octanol + NAD+
octanal + NADH + H+
substrate for isozyme ADH3
-
-
r
1-octanol + NAD+
octanal + NADH + H+
-
33% of the activity with 2-propanol, in the reverse reaction 435% of the activity with phenyl trifluoromethyl ketone
-
-
r
1-octanol + NAD+
octanal + NADH + H+
about 85% of activity with ethanol, ADH1
-
-
?
1-octanol + NAD+
octanal + NADH + H+
11% activity compared to benzyl alcohol
-
-
?
1-octanol + NAD+
octanal + NADH + H+
57% activity compared to cyclohexanol
-
-
r
1-pentanol + NAD+
pentanal + NADH + H+
about 85% of activity with ethanol, ADH1
-
-
?
1-pentanol + NAD+
pentanal + NADH + H+
152% activity compared to benzyl alcohol
-
-
?
1-pentanol + NAD+
pentanal + NADH + H+
19.1% activity compared to ethanol
-
-
?
1-pentanol + NAD+
pentanal + NADH + H+
121% activity compared to cyclohexanol
-
-
r
1-phenyl-1,2-propanedione + NADH + H+
?
1-phenyl-1,2-propanedione and ethyl 3-methyl-2-oxobutyrate are the best substrate in the reduction reaction
-
-
?
1-phenyl-1,2-propanedione + NADH + H+
?
1-phenyl-1,2-propanedione and ethyl 3-methyl-2-oxobutyrate are the best substrate in the reduction reaction
-
-
?
1-phenyl-1,2-propanedione + NADH + H+
?
-
activity is 1.46fold higher than with 2,2,2-trifluoroacetophenone
-
-
?
1-phenyl-2-butanone + NADH + H+
1-phenylbutan-2-ol + NAD+
-
1.5fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
1-phenyl-2-butanone + NADH + H+
1-phenylbutan-2-ol + NAD+
-
1.5fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
1-phenyl-2-butanone + NADH + H+
1-phenylbutan-2-ol + NAD+
-
12% of the activity with phenyl trifluoromethyl ketone
-
-
?
1-phenyl-2-propanol + NAD+
1-phenyl-2-propanone + NADH + H+
39% of the activity with 1-phenylethanol
-
-
?
1-phenyl-2-propanol + NAD+
1-phenyl-2-propanone + NADH + H+
3% activity compared to cyclohexanol
-
-
r
1-phenyl-2-propanol + NAD+
1-phenyl-2-propanone + NADH + H+
-
16% of the activity with (S)-(-)-1-phenylethanol
-
-
?
1-phenylethanol + NAD+
1-phenylethanone + NADH
-
46% of the activity with 2-phenylethanol
-
-
?
1-phenylethanol + NAD+
1-phenylethanone + NADH + H+
3% activity compared to cyclohexanol
-
-
r
1-propanol + NAD+
propanal + NADH + H+
the enzyme shows a preference for short-chain alcohols ethanol and 1-propanol
-
-
?
1-propanol + NAD+
propanal + NADH + H+
the enzyme shows a preference for short-chain alcohols ethanol and 1-propanol
-
-
?
1-propanol + NAD+
propanal + NADH + H+
about 75% of activity with ethanol, ADH1
-
-
?
1-propanol + NAD+
propanal + NADH + H+
153% activity compared to cyclohexanol
-
-
r
12-hydroxydodecanoate + NAD+
12-oxododecanoic acid + NADH
-
-
-
-
?
12-hydroxydodecanoate + NAD+
12-oxododecanoic acid + NADH
-
oxidized at pH 10, not oxidized at pH 7.5
-
-
-
13-cis-retinol + NAD+
13-cis-retinal + NADH
-
no activity with isozyme ADH1
-
-
?
13-cis-retinol + NAD+
13-cis-retinal + NADH
-
no activity with isozyme ADH1
-
-
?
2,2,2-trifluoroacetophenone + NADH + H+
(R)-alpha-(trifluoromethyl)benzyl alcohol + NAD+
-
-
93% enantiomeric excess
-
r
2,2,2-trifluoroacetophenone + NADH + H+
(R)-alpha-(trifluoromethyl)benzyl alcohol + NAD+
-
93% enantiomeric excess
-
-
?
2,2,2-trifluoroacetophenone + NADH + H+
2,2,2-trifluoro-1-phenylethanol + NAD+
35% of the activity compared to 1-phenyl-1,2-propanedione
-
-
?
2,2,2-trifluoroacetophenone + NADH + H+
2,2,2-trifluoro-1-phenylethanol + NAD+
-
-
-
-
r
2,2-dichloroacetophenone + NADH + H+
2,2-dichloro-1-phenylethanol + NAD+
30% of the activity compared to 1-phenyl-1,2-propanedione
-
-
?
2,2-dichloroacetophenone + NADH + H+
2,2-dichloro-1-phenylethanol + NAD+
-
32% of the activity with 2,2,2-trifluoroacetophenone
-
-
?
2,3-butanediol + NAD+
acetoin + NADH + H+
272% of the activity with 1-phenylethanol
-
-
r
2,4-pentanediol + NAD+
?
-
21% of the activity with (S)-N-benzyl-3-pyrrolidinol
-
-
?
2-(3,5-dimethylphenyl)propanal + NADH + H+
(S)-2-(3,5-dimethylphenyl)propanol + NAD+
-
18 h, 99% yield, 90% enantiomeric excess
-
-
?
2-(3,5-dimethylphenyl)propanal + NADH + H+
(S)-2-(3,5-dimethylphenyl)propanol + NAD+
18 h, 99% yield, 90% enantiomeric excess
-
-
?
2-(3-benzoylphenyl)propanal + NADH + H+
(S)-2-(3-benzoylphenyl)propanol + NAD+
-
18 h, 85% yield, 95% enantiomeric excess
-
-
?
2-(3-benzoylphenyl)propanal + NADH + H+
(S)-2-(3-benzoylphenyl)propanol + NAD+
18 h, 85% yield, 95% enantiomeric excess
-
-
?
2-(3-fluorobiphenyl-4-yl)propanal + NADH + H+
(S)-2-(3-(fluoro)biphenyl-4-yl)propanol + NAD+
-
18 h, 77% yield, 97% enantiomeric excess
-
-
?
2-(3-fluorobiphenyl-4-yl)propanal + NADH + H+
(S)-2-(3-(fluoro)biphenyl-4-yl)propanol + NAD+
18 h, 77% yield, 97% enantiomeric excess
-
-
?
2-(3-phenoxyphenyl)propanal + NADH + H+
(S)-2-((3-phenoxy)phenyl)propanol + NAD+
-
18 h, 85% yield, 95% enantiomeric excess
-
-
?
2-(3-phenoxyphenyl)propanal + NADH + H+
(S)-2-((3-phenoxy)phenyl)propanol + NAD+
18 h, 85% yield, 95% enantiomeric excess
-
-
?
2-(4-isobutylphenyl)propanal + NADH + H+
(S)-2-(4-isobutylphenyl)propanol + NAD+
-
18 h, 92% yield, 99% enantiomeric excess
-
-
?
2-(4-isobutylphenyl)propanal + NADH + H+
(S)-2-(4-isobutylphenyl)propanol + NAD+
18 h, 92% yield, 99% enantiomeric excess
-
-
?
2-butanol + NAD+
2-butanone + NADH + H+
-
activity is 3.7fold higher than with (S)-N-benzyl-3-pyrrolidinol
-
-
r
2-butanol + NAD+
2-butanone + NADH + H+
weak activity
-
-
r
2-butanol + NAD+
2-butanone + NADH + H+
about 25% of activity with ethanol, ADH1
-
-
?
2-butanol + NAD+
2-butanone + NADH + H+
39% activity compared to cyclohexanol
4% activity compared to cyclohexanone
-
r
2-butanone + NADH + H+
2-butanol + NAD+
-
40% of the activity with N-benzyl-3-pyrrolidinone
-
-
r
2-butanone + NADPH + H+
butan-2-ol + NADP+
12.1% of the activity with 2-hydroxyacetophenone and NADPH
-
-
?
2-butanone + NADPH + H+
butan-2-ol + NADP+
12.1% of the activity with 2-hydroxyacetophenone and NADPH
-
-
?
2-heptanol + NAD+
2-heptanone + NADH + H+
weak activity
-
-
r
2-heptanol + NAD+
2-heptanone + NADH + H+
63% activity compared to cyclohexanol
5% activity compared to cyclohexanone
-
r
2-heptanone + NADPH + H+
heptan-2-ol + NADP+
6.8% of the activity with 2-hydroxyacetophenone and NADPH
-
-
?
2-heptanone + NADPH + H+
heptan-2-ol + NADP+
6.8% of the activity with 2-hydroxyacetophenone and NADPH
-
-
?
2-hexanol + NAD+
2-hexanone + NADH + H+
-
activity is 11.2fold higher than with (S)-N-benzyl-3-pyrrolidinol
-
-
?
2-hexanol + NAD+
2-hexanone + NADH + H+
weak activity
-
-
r
2-hexanol + NAD+
2-hexanone + NADH + H+
64% activity compared to cyclohexanol
4% activity compared to cyclohexanone
-
r
2-hexanone + NADPH + H+
hexan-2-ol + NADP+
5.9% of the activity with 2-hydroxyacetophenone and NADPH
-
-
?
2-hexanone + NADPH + H+
hexan-2-ol + NADP+
5.9% of the activity with 2-hydroxyacetophenone and NADPH
-
-
?
2-hydroxyacetophenone + NADH + H+
(S)-1-phenyl-1,2-ethanediol + NAD+
2.4% of the activity with NADPH
-
-
?
2-hydroxyacetophenone + NADH + H+
(S)-1-phenyl-1,2-ethanediol + NAD+
2.4% of the activity with NADPH
-
-
?
2-methylpropan-1-ol + NAD+
2-methyl-propan-1-one + NADH
-
-
-
-
?
2-methylpropan-1-ol + NAD+
2-methyl-propan-1-one + NADH + H+
-
-
-
?
2-methylpropan-1-ol + NAD+
2-methyl-propan-1-one + NADH + H+
-
-
-
-
?
2-octanol + NAD+
2-octanone + NADH + H+
weak activity
-
-
r
2-octanol + NAD+
2-octanone + NADH + H+
43% activity compared to cyclohexanol
4% activity compared to cyclohexanone
-
r
2-oxo-3-methylpentane + NADH
3-methylpentan-2-ol + NAD+
-
-
-
-
?
2-oxo-3-methylpentane + NADH
3-methylpentan-2-ol + NAD+
-
-
-
-
?
2-oxo-3-phenylpropane + NADH
2-hydroxy-3-phenylpropane + NAD+
-
-
-
-
?
2-oxo-3-phenylpropane + NADH
2-hydroxy-3-phenylpropane + NAD+
-
-
-
-
?
2-pentanol + NAD+
2-pentanone + NADH + H+
-
45% of activity with N-benzyl-3-pyrrolidinol
-
-
?
2-pentanol + NAD+
2-pentanone + NADH + H+
-
45% of activity with N-benzyl-3-pyrrolidinol
-
-
?
2-pentanol + NAD+
2-pentanone + NADH + H+
-
activity is 9fold higher than with (S)-N-benzyl-3-pyrrolidinol
-
-
?
2-pentanol + NAD+
2-pentanone + NADH + H+
weak activity
-
-
r
2-pentanol + NAD+
2-pentanone + NADH + H+
5.7% activity compared to ethanol
-
-
?
2-pentanone + NADH + H+
2-pentanol + NAD+
6% activity compared to cyclohexanol
-
-
r
2-propanol + NAD+
2-propanone + NADH
-
54% of the activity with 2-phenylethanol
-
-
?
2-propanol + NAD+
2-propanone + NADH + H+
-
activity is 3.1fold higher than with (S)-N-benzyl-3-pyrrolidinol
-
-
?
2-propanol + NAD+
2-propanone + NADH + H+
73.5% activity compared to ethanol
-
-
?
2-propanol + NAD+
2-propanone + NADH + H+
6% activity compared to cyclohexanol
-
-
r
2-propanol + NAD+
acetone + NADH + H+
about 50% of activity with ethanol, ADH1
-
-
?
2-propanol + NAD+
acetone + NADH + H+
about 50% of activity with ethanol, ADH1
-
-
?
3-methoxybenzyl alcohol + NAD+
3-methoxybenzaldehyde + NADH + H+
-
-
-
-
?
3-methoxybenzyl alcohol + NAD+
3-methoxybenzaldehyde + NADH + H+
-
13% of the activity with (S)-(-)-1-phenylethanol
-
-
?
3-methylbutan-1-ol + NAD+
3-methyl-butan-1-one + NADH + H+
-
-
-
?
3-methylbutan-1-ol + NAD+
3-methyl-butan-1-one + NADH + H+
-
-
-
-
?
3-methylbutanal + NAD+
? + NADH + H+
about 10% of the activity with ethanol or 1-propanol
-
-
?
3-methylbutanal + NAD+
? + NADH + H+
about 10% of the activity with ethanol or 1-propanol
-
-
?
3-methylcyclohexanone + NADH
3-methylcyclohexanol + NAD+
about 10% of the activity compared to isatin
-
-
?
3-methylcyclohexanone + NADH
3-methylcyclohexanol + NAD+
about 10% of the activity compared to isatin
-
-
?
3-nitrobenzaldehyde + NADH + H+
3-nitrobenzyl alcohol + NAD+
-
class IV isozyme, reductive activity
-
-
?
3-oxo-5beta-androstan-17beta-ol + NADH
3beta,17beta-dihydroxy-5beta-androstane + NAD+
-
-
-
-
?
3-oxo-5beta-androstan-17beta-ol + NADH
3beta,17beta-dihydroxy-5beta-androstane + NAD+
-
-
-
-
?
3-pentanol + NAD+
3-pentanone + NADH + H+
2% activity compared to cyclohexanol
2% activity compared to cyclohexanone
-
r
3beta-hydroxy-5beta-androstan-17-one + NAD+
5beta-androstan-3,17-dione + NADH
-
-
-
-
?
3beta-hydroxy-5beta-androstan-17-one + NAD+
5beta-androstan-3,17-dione + NADH
-
catalyzed by isoenzyme BB-ADH, no activity with isoenzyme AA-ADH and TT-ADH
-
-
?
3beta-hydroxy-5beta-androstan-17-one + NAD+
5beta-androstan-3,17-dione + NADH
-
-
-
-
-
4-chloroacetophenone + NADH
1-(4-chlorophenyl)ethanol + NAD+
-
-
-
-
r
4-methoxybenzyl alcohol + NAD+
4-methoxybenzaldehyde + NADH + H+
-
-
-
-
r
4-methoxybenzyl alcohol + NAD+
4-methoxybenzaldehyde + NADH + H+
-
99% of the activity with (S)-(-)-1-phenylethanol
-
-
?
4-methoxybenzyl alcohol + NAD+
4-methoxybenzaldehyde + NADH + H+
-
99% of the activity with (S)-1-phenylethanol
-
-
r
4-methyl-1-pentanol + NAD+
4-methyl-1-pentanal + NADH
-
-
-
-
?
4-nitrobenzaldehyde + NADH + H+
4-nitrobenzyl alcohol + NAD+
-
-
-
-
r
4-nitrobenzaldehyde + NADH + H+
4-nitrobenzyl alcohol + NAD+
-
-
-
-
?
5alpha-androstan-17beta-ol-3-one + NADH + H+
3beta,17beta-dihydroxy-5alpha-androstan + NAD+
-
-
-
-
-
5alpha-androstan-17beta-ol-3-one + NADH + H+
3beta,17beta-dihydroxy-5alpha-androstan + NAD+
-
-
-
-
?
5beta-androstan-17beta-ol-3-one + NAD+
5beta-androstan-3,17-dione + NADH
-
-
-
-
?
5beta-androstan-17beta-ol-3-one + NAD+
5beta-androstan-3,17-dione + NADH
-
low activity
-
-
?
5beta-androstan-3beta-ol-17-one + NAD+
5beta-androstan-3,17-dione + NADH
-
-
-
-
?
5beta-androstan-3beta-ol-17-one + NAD+
5beta-androstan-3,17-dione + NADH
-
-
-
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
-
the reduction of acetaldehyde is 4.9fold faster than the oxidation of ethanol
-
-
r
acetaldehyde + NADH + H+
ethanol + NAD+
-
-
100% of the activity with butan-2-ol
-
r
acetaldehyde + NADH + H+
ethanol + NAD+
-
-
-
r
acetaldehyde + NADH + H+
ethanol + NAD+
-
-
-
r
acetaldehyde + NADH + H+
ethanol + NAD+
-
-
-
r
acetaldehyde + NADH + H+
ethanol + NAD+
-
-
-
r
acetaldehyde + NADH + H+
ethanol + NAD+
-
reduced by isoenzyme A2 and C2, no activity with isoenzyme B2
-
-
-
acetaldehyde + NADH + H+
ethanol + NAD+
-
cells with an extra copy of ADH1 display chronological life-span extension. Antioxidant enzymes are induced in 2xADH1 cells. Strains carrying an extra ADH1 copy show extended replicative life span and increased Sir2p activity
-
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
mutant enzyme S109P/L116S/Y294C
-
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
-
-
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
-
reduced at the highest rate of all aldehydes tested
-
-
acetaldehyde + NADH + H+
ethanol + NAD+ + H+
-
-
-
r
acetaldehyde + NADH + H+
ethanol + NAD+ + H+
-
-
-
?
acetaldehyde + NADH + H+
ethanol + NAD+ + H+
-
-
-
?
acetaldehyde + NADPH + H+
ethanol + NADP+
-
NADPH is not a cofactor for wild-type, but for mutant P704L/H734R
-
-
r
acetaldehyde + NADPH + H+
ethanol + NADP+
Ruminiclostridium thermocellum DSM 1237
-
NADPH is not a cofactor for wild-type, but for mutant P704L/H734R
-
-
r
acetaldehyde + NADPH + H+
ethanol + NADP+
-
-
-
?
acetaldehyde + NADPH + H+
ethanol + NADP+
-
-
-
?
acetophenone + NADH + H+
1-phenylethanol + NAD+
-
1.8fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
acetophenone + NADH + H+
1-phenylethanol + NAD+
-
40% of the activity with N-benzyl-3-pyrrolidinone
-
-
?
acetophenone + NADH + H+
1-phenylethanol + NAD+
-
-
-
?
acetophenone + NADPH + H+
1-phenylethanol + NADP+
5.1% of the activity with 2-hydroxyacetophenone and NADPH
-
-
?
acetophenone + NADPH + H+
1-phenylethanol + NADP+
5.1% of the activity with 2-hydroxyacetophenone and NADPH
-
-
?
alcohol + NAD+
aldehyde or ketone + NADH
-
medium chain sec-alcohols or (omega-1)-ketones, no activity with primary alcohols or aldehydes
-
-
r
alcohol + NAD+
aldehyde or ketone + NADH
-
medium chain sec-alcohols or (omega-1)-ketones, no activity with primary alcohols or aldehydes
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH
-
ADH4 might be involved in biosynthesis of retinoic acid
-
-
r
allyl alcohol + NAD+
acrolein + NADH
-
-
product is toxic in mouse hepatocytes due to cell protein carbonylation following exposure to crotyl alcohol
-
?
alpha-tetralone + NADH + H+
(S)-alpha-tetralol + NAD+
-
-
99% enantiomeric excess
-
r
alpha-tetralone + NADH + H+
(S)-alpha-tetralol + NAD+
-
more than 99% enantiomeric excess
-
-
?
benzaldehyde + NADH
benzyl alcohol + NAD+
-
reduced by isoenzyme A2 and C2, no activity with isoenzyme B2
-
-
r
benzaldehyde + NADH + H+
benzyl alcohol + NAD+
-
1.2% of the activity with acetaldehyde
-
-
?
benzaldehyde + NADH + H+
benzyl alcohol + NAD+
-
21% of activity with N-benzyl-3-pyrrolidinone
-
-
?
benzaldehyde + NADH + H+
benzyl alcohol + NAD+
-
74% of the activity with N-benzyl-3-pyrrolidinone
-
-
?
benzaldehyde + NADH + H+
benzyl alcohol + NAD+
-
-
93% of the activity with butan-2-ol
-
r
benzaldehyde + NADH + H+
benzyl alcohol + NAD+
3% activity compared to benzyl alcohol
-
-
r
benzaldehyde + NADH + H+
benzyl alcohol + NAD+
-
14% of the activity with 2,2,2-trifluoroacetophenone
-
-
?
benzaldehyde + NADPH + H+
benzyl alcohol + NADP+
107% of the activity with (2E)-but-2-enal, yield 99% after 12 h
-
-
r
benzaldehyde + NADPH + H+
benzyl alcohol + NADP+
107% of the activity with (2E)-but-2-enal, yield 99% after 12 h
-
-
r
benzyl alcohol + NAD+
benzaldehyde + NADH
-
oxidized by isoenzyme A2 and C2 no activity with isoenzyme B2
-
-
?
benzyl alcohol + NAD+
benzaldehyde + NADH
-
oxidation with isoenzyme ADH-1 and ADH-3, no activity with isoenzyme ADH-2
-
-
?
benzyl alcohol + NAD+
benzaldehyde + NADH + H+
-
199% of the activity with 2-phenylethanol
-
-
?
benzyl alcohol + NAD+
benzaldehyde + NADH + H+
-
-
-
-
?
benzyl alcohol + NAD+
benzaldehyde + NADH + H+
-
-
33% of the activity with butan-2-ol
-
r
benzyl alcohol + NAD+
benzaldehyde + NADH + H+
-
-
-
-
r
benzyl alcohol + NAD+
benzaldehyde + NADH + H+
-
178% activity compared to cyclohexanone
-
r
benzyl alcohol + NAD+
benzaldehyde + NADH + H+
47% activity compared to cyclohexanol
154% activity compared to cyclohexanone
-
r
benzylacetone + NADH + H+
4-phenylbutan-2-ol + NAD+
-
activity is 1.3fold higher than with N-benzyl-3-pyrrolidinone
-
-
?
benzylalcohol + NAD+
benzaldehyde + NADH + H+
weak activity
-
-
r
butan-2-ol + NAD+
butan-2-one + NADH
-
(R)-2-butanol and (S)-2-butanol
-
?
butanol + NAD+
1-butanal + NADH + H+
about 15% of the activity with ethanol or 1-propanol
-
-
?
butanol + NAD+
1-butanal + NADH + H+
about 15% of the activity with ethanol or 1-propanol
-
-
?
butanol + NAD+
butyraldehyde + NADH
-
pH 10.0: oxidized by ADH-1 and ADH-3, no activity with isoenzyme ADH-2
-
-
?
butanol + NAD+
butyraldehyde + NADH
-
activity with ADH I, no activity with ADH II
-
-
?
butanol + NAD+
butyraldehyde + NADH
-
oxidized by enzyme form ADH-I, no activity with enzyme form ADH-II
-
-
-
butanol + NAD+
butyraldehyde + NADH + H+
-
immobilized HLAD shows about 95% reaction rate and free HLAD shows about 90% reaction rate with butanol compared to ethanol at pH 8.8 and 30°C
-
-
?
butanol + NAD+
butyraldehyde + NADH + H+
-
359% activity compared to cyclohexanone
-
r
butyraldehyde + NADH
n-butanol + NAD+
-
activity with enzyme form ADH I, no activity with enzyme form ADH II
-
r
butyraldehyde + NADH + H+
n-butanol + NAD+
-
best substrate for isozyme ADH II
-
-
r
butyraldehyde + NADH + H+
n-butanol + NAD+
Acetobacter pasteurianus SKU1108
-
best substrate for isozyme ADH II
-
-
r
chloroacetone + NADH + H+
1-chloropropan-2-ol + NAD+
-
41.7fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
chloroacetone + NADH + H+
1-chloropropan-2-ol + NAD+
-
238% of the activity with phenyl trifluoromethyl ketone
-
-
?
crotyl alcohol + NAD+
crotonaldehyde + NADH
-
product is toxic in mouse hepatocytes due to cell protein carbonylation following exposure to crotyl alcohol
-
-
?
crotyl alcohol + NAD+
crotonaldehyde + NADH
-
-
product is toxic in mouse hepatocytes due to cell protein carbonylation following exposure to crotyl alcohol
-
?
cycloheptanol + NAD+
cycloheptanone + NADH + H+
37% of activity compared to (S)-1-indanol
-
-
?
cycloheptanone + NADH
cycloheptanol + NAD+
-
-
-
-
?
cyclohexanol + NAD+
cyclohexanone + NADH
-
reaction is catalyzed by the cathodic pyrazole-sensitive enzyme, no activity with the cathodic pyrazole-insensitive enzyme and by the anodic pyrazole-insensitive enzyme
-
-
?
cyclohexanol + NAD+
cyclohexanone + NADH
-
oxidized by isoenzyme A2, no activity with isoenzymes B2 and C2
-
-
?
cyclohexanol + NAD+
cyclohexanone + NADH + H+
12% of the activity with 2,3-butanediol
-
-
r
cyclohexanol + NAD+
cyclohexanone + NADH + H+
-
-
-
-
?
cyclohexanol + NAD+
cyclohexanone + NADH + H+
52% of the activity with 1-phenylethanol
-
-
?
cyclohexanol + NAD+
cyclohexanone + NADH + H+
100% activity
100% activity
-
r
cyclohexanol + NAD+
cyclohexanone + NADH + H+
-
13% of the activity with (S)-(-)-1-phenylethanol
-
-
?
cyclohexanone + NADH
cyclohexanol + NAD+
-
best cyclic ketone substrate
-
-
?
cyclohexanone + NADH + H+
cyclohexanol + NAD+
38% of the activity with acetoin
-
-
r
cyclohexanone + NADH + H+
cyclohexanol + NAD+
-
-
-
?
cyclopentanol + NAD+
cyclopentanone + NADH + H+
-
-
92% of the activity with butan-2-ol
-
?
cyclopentanol + NAD+
cyclopentanone + NADH + H+
55% of the activity compared to isoborneol
-
-
?
diacetyl + NADH + H+
?
-
16.1fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
diacetyl + NADH + H+
?
-
16.1fold higher activity compared to activity with N-benzyl-3-pyrrolidinone
-
-
?
ethanol + 2 NAD+ + H2O
acetic acid + 2 NADH + 2 H+
best substrate
-
-
r
ethanol + 2 NAD+ + H2O
acetic acid + 2 NADH + 2 H+
about 45% of the activity with 1-octanol
-
-
r
ethanol + NAD+
acetaldehyde + NADH
-
-
acetaldehyde is the best substrate for isozyme ADH I
-
r
ethanol + NAD+
acetaldehyde + NADH
Acetobacter pasteurianus SKU1108
-
-
acetaldehyde is the best substrate for isozyme ADH I
-
r
ethanol + NAD+
acetaldehyde + NADH
-
76% of the activity with 2-phenylethanol
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
76% of the activity with 2-phenylethanol
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
the reduction of acetaldehyde of ADH-MII is about 7times higher than that of the oxidation of ethanol
-
r
ethanol + NAD+
acetaldehyde + NADH
Candida sp. N-16
-
the reduction of acetaldehyde of ADH-MII is about 7times higher than that of the oxidation of ethanol
-
r
ethanol + NAD+
acetaldehyde + NADH
-
no cooperativity between the 2 active sites of the enzyme
-
-
r
ethanol + NAD+
acetaldehyde + NADH
-
the reduction of acetaldehyde is 4.9fold faster than the oxidation of ethanol
-
r
ethanol + NAD+
acetaldehyde + NADH
-
plays an important role in the metabolism of ethanol
-
-
?
ethanol + NAD+
acetaldehyde + NADH
isomerization of the enzyme-NAD+ complex is the rate-limiting step for acetaldehyde reduction by the wild-type enzyme
-
-
r
ethanol + NAD+
acetaldehyde + NADH
proton and hydride equivalent transfer in the alcohol dehydrogenase enzymatic reaction are modulated by the correlated motions between NAD+ and the cofactor domain
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
-
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
class III isoenzyme chi-ADH oxidizes ethanol very poorly
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
chi-ADH plays an important role in the metabolism of long chain alcohols and aldehydes
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
the anodic enzyme form may contribute significantly to alcohol elimination in man, particularly at high concentrations when the other enzyme species are saturated
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
the enzyme plays a significant role in first-pass metabolism of ethanol in human
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
enzyme is responsible for the major ethanol oxidation capacity in the body. The products acetaldehyde and NADH are responsible for the most of the toxic effects and metabolic disturbances produced by ethanol ingestion
-
?
ethanol + NAD+
acetaldehyde + NADH
-
no activity with isoenzyme B2, oxidized by isoenzyme A2 and C2
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
role of the major liver isoenzyme A2 in ethanol metabolism
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
DH3 plays an important role in systemic ethanol metabolism at higher levels of blood ethanol through activation by cytoplasmic solution hydrophobicity
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
isoenzyme ADH-1 and ADH-3, no activity with isoenzyme ADH-2
-
-
ethanol + NAD+
acetaldehyde + NADH
-
rate-limiting step of the alcoholic fermentation
-
-
?
ethanol + NAD+
acetaldehyde + NADH + H+
-
no activity with NADP+, in reverse reaction no activity with NADPH
-
-
r
ethanol + NAD+
acetaldehyde + NADH + H+
-
-
83% of the activity with butan-2-ol
-
r
ethanol + NAD+
acetaldehyde + NADH + H+
the enzyme shows a preference for short-chain alcohols ethanol and 1-propanol
-
-
?
ethanol + NAD+
acetaldehyde + NADH + H+
the enzyme shows a preference for short-chain alcohols ethanol and 1-propanol
-
-
?
ethanol + NAD+
acetaldehyde + NADH + H+
substrate for isozyme ADH1C, extremely poor substrate for isozyme ADH3
-
-
r
ethanol + NAD+
acetaldehyde + NADH + H+
substrate for isozyme ADH2
-
-
r
ethanol + NAD+
acetaldehyde + NADH + H+
substrate for isozyme ADH4
-
-
r
ethanol + NAD+
acetaldehyde + NADH + H+
-
-
-
r
ethanol + NAD+
acetaldehyde + NADH + H+
-
-
-
r
ethanol + NAD+
acetaldehyde + NADH + H+
-
the enzyme is highly specific for ethanol with NAD+ as the coenzyme
-
-
r
ethanol + NAD+
acetaldehyde + NADH + H+
-
-
-
-
?
ethanol + NAD+
acetaldehyde + NADH + H+
-
-
-
-
?
ethanol + NAD+
acetaldehyde + NADH + H+
88% activity compared to cyclohexanol
-
-
r
ethanol + NADP+
acetaldehyde + NADPH + H+
8.5% of the activity with ethanol and NAD+
-
-
?
ethyl benzoylformate + NADH + H+
ethyl (R)-mandelate + NAD+
-
50% enantiomeric excess
-
r
ethyl benzoylformate + NADH + H+
ethyl (R)-mandelate + NAD+
-
50% enantiomeric excess
-
r
ethyl pyruvate + NADH
?
about 15% of the activity compared to isatin
-
-
?
ethyl pyruvate + NADH
?
about 15% of the activity compared to isatin
-
-
?
ethylene glycol + NAD+
? + NADH
-
class III isoenzyme chi-ADH shows no activity
-
-
-
ethylene glycol + NAD+
? + NADH
-
oxidized by isoenzyme A2, no activity with isoenzyme B2 and C2
-
-
?
formaldehyde + NADH + H+
methanol + NAD+
-
reduced by isoenzyme A2, no activity with isoenzyme B2 and C2
-
-
r
formaldehyde + NADH + H+
methanol + NAD+
-
activity with ADH I, no activity with ADH II
-
-
?
furfuryl alcohol + NAD+
furfural + NADH
-
activity with ADH I, no activity with ADH II
-
r
hexanol + NAD+
n-hexanal + NADH
-
activity with ADH I, no activity with ADH II
-
-
-
isopropanol + 2 NAD+ + H2O
? + 2 NADH + 2 H+
about 10% of the activity with 1-octanol
-
-
r
isopropanol + 2 NAD+ + H2O
? + 2 NADH + 2 H+
about 15% of the activity with 1-octanol
-
-
r
m-nitrobenzaldehyde + NADH + H+
m-nitrobenzyl alcohol + NAD+
-
substrate of class IV ADH isozyme
-
-
r
m-nitrobenzaldehyde + NADH + H+
m-nitrobenzyl alcohol + NAD+
-
-
-
-
methanol + NAD+
formaldehyde + NADH + H+
-
anodic enzyme form shows no activity
-
-
-
methanol + NAD+
formaldehyde + NADH + H+
-
no activity with isoenzyme beta3,beta3
-
-
?
methanol + NAD+
formaldehyde + NADH + H+
-
activity detected with class II isoenzyme pi-ADH
-
-
-
methanol + NAD+
formaldehyde + NADH + H+
-
oxidized by isoenzyme beta1,beta1
-
-
?
methanol + NAD+
formaldehyde + NADH + H+
-
class III isoenzyme chi-ADH shows no activity
-
-
-
methanol + NAD+
formaldehyde + NADH + H+
-
no activity with class III enzyme
-
-
-
methanol + NAD+
formaldehyde + NADH + H+
-
reaction is catalyzed by the cathodic pyrazole-sensitive enzyme, no activity by the cathodic pyrazole-insensitive enzyme and by the anodic pyrazole-insensitive enzyme
-
-
?
methanol + NAD+
formaldehyde + NADH + H+
-
no activity
-
-
-
methanol + NAD+
formaldehyde + NADH + H+
-
weak activity with isoenzyme A2, no activity with isoenzyme B2 and C2
-
-
?, r
methanol + NAD+
formaldehyde + NADH + H+
-
no activity at pH 7.5, slight activity at pH 10.8
-
-
?
methanol + NAD+
formaldehyde + NADH + H+
-
oxidized with ADH-3, no activity with ADH-1 and ADH-2
-
-
?
methanol + NAD+
formaldehyde + NADH + H+
-
reaction is catalyzed by the pyrazole-sensitive enzyme, no activity with the pyrazole-insensitive enzyme
-
-
?
methanol + NAD+
formaldehyde + NADH + H+
49.9% activity compared to ethanol
-
-
?
methyl benzoylformate + NADH
?
about 35% of the activity compared to isatin
-
-
?
methyl benzoylformate + NADH
?
about 35% of the activity compared to isatin
-
-
?
N-benzyl-3-pyrrolidinone + NADH + H+
(S)-N-benzyl-3-pyrrolidinol + NAD+
-
-
-
-
r
N-benzyl-3-pyrrolidinone + NADH + H+
(S)-N-benzyl-3-pyrrolidinol + NAD+
-
(S)-N-benzyl-3-pyrrolidinol is produced at an enantiomeric excess of more than 99.9%
-
-
r
octan-1-ol + NAD+
n-octanal + NADH
-
activity with ADH I, no activity with ADH II
-
-
?
octanal + NAD+ + H2O
octanoic acid + NADH + H+
about 25% of the activity with 1-octanol
-
-
r
octanal + NAD+ + H2O
octanoic acid + NADH + H+
about 25% of the activity with 1-octanol
-
-
r
octanol + NAD+
octanal + NADH + H+
-
immobilized and free HLAD show 100% reaction rate with octanol compared to ethanol at pH 8.8 and 30°C
-
-
?
octanol + NAD+
octanal + NADH + H+
-
178% activity compared to cyclohexanone
-
r
p-methoxybenzyl alcohol + NAD+
p-methoxybenzaldehyde + NADH + H+
-
-
-
r
p-methoxybenzyl alcohol + NAD+
p-methoxybenzaldehyde + NADH + H+
-
-
-
-
r
pentan-2-ol + NAD+
2-pentanone + NADH
-
(R)-2-pentanol and (S)-2-pentanol
-
r
pentan-2-ol + NAD+
pentan-2-one + NADH + H+
-
-
93% of the activity with butan-2-ol
-
?
pentan-2-ol + NAD+
pentan-2-one + NADH + H+
-
9% of the activity with 2,3-butanediol
-
?
pentanol + NAD+
n-pentanal + NADH
-
activity with ADH I, no activity with ADH II
-
-
?
pentanol + NAD+
pentanone + NADH
-
-
-
-
?
pentanol + NAD+
pentanone + NADH
-
oxidized by isoenzyme A2 and B2, no activity with isoenzyme C2
-
-
?
primary or secondary alcohol + NAD+
aldehyde or ketone + NADH
-
-
-
-
r
primary or secondary alcohol + NAD+
aldehyde or ketone + NADH
-
-
-
-
r
propan-2-ol + NAD+
acetone + NADH
-
3% of the activity with ethanol
-
-
-
propan-2-ol + NAD+
acetone + NADH + H+
-
-
synthesis of [4R-(2)H]NADH with high yield by enzymatic oxidation of 2-propanol-d(8)
-
?
propan-2-ol + NAD+
acetone + NADH + H+
-
6% activity compared to cyclohexanone
-
r
propionaldehyde + NADH
propanol + NAD+
-
94% of the activity with acetaldehyde
-
-
?
trans-cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
-
% of the activity with phenyl trifluoromethyl ketone
-
-
?
additional information
?
-
-
substrate specificity of the 2 isozmyes with various substrates, overview, isozymes are highly specific for the (R)-stereoisomers and enantioselctive for the R(-)isomers
-
-
-
additional information
?
-
Acetobacter pasteurianus SKU1108
-
substrate specificity of the 2 isozmyes with various substrates, overview, isozymes are highly specific for the (R)-stereoisomers and enantioselctive for the R(-)isomers
-
-
-
additional information
?
-
-
the enzyme shows broad substrate specificity and prefers aliphatic alcohols and ketones. There are no large differences in the reactivities between primary and secondary alcohols. The enzyme produces (S)-alcohols from the corresponding ketones. The values of the enantiomeric excess increase with the increase of chain length except for the reduction of 2-hexanone. The highest enantioselectivity is shown with the reduction of 2-nonanone
-
-
-
additional information
?
-
Aeropyrum pernix DSM 11879
-
the enzyme shows broad substrate specificity and prefers aliphatic alcohols and ketones. There are no large differences in the reactivities between primary and secondary alcohols. The enzyme produces (S)-alcohols from the corresponding ketones. The values of the enantiomeric excess increase with the increase of chain length except for the reduction of 2-hexanone. The highest enantioselectivity is shown with the reduction of 2-nonanone
-
-
-
additional information
?
-
-
substrate specificity and enantiospecificity, overview. The (R)-specific alcohol dehydrogenase requires NADH and reduces various kinds of carbonyl compounds, including ketones and aldehydes. AFPDH reduces acetylpyridine derivatives, beta-keto esters, and some ketones compounds with high enantiospecificity, overview. No activity with 2-chlorobenzaldehyde and 2-tetralone, poor activity with 1-tetralone, pyruvate, 2-oxobutyrate, oxalacetate, cyclopentanone, cyclohexanone, cycloheptanone, and dipropylketone. No activity with 1,2-propanediol, 3-chloro-1,2-propanediol, 3-bromo-1,2-propanediol, glycerol, 1-pentanol, poor activity with 1-butanol, 1-propanol, ethanol, and methanol
-
-
-
additional information
?
-
-
substrate specificity and enantiospecificity, overview. The (R)-specific alcohol dehydrogenase requires NADH and reduces various kinds of carbonyl compounds, including ketones and aldehydes. AFPDH reduces acetylpyridine derivatives, beta-keto esters, and some ketones compounds with high enantiospecificity, overview. No activity with 2-chlorobenzaldehyde and 2-tetralone, poor activity with 1-tetralone, pyruvate, 2-oxobutyrate, oxalacetate, cyclopentanone, cyclohexanone, cycloheptanone, and dipropylketone. No activity with 1,2-propanediol, 3-chloro-1,2-propanediol, 3-bromo-1,2-propanediol, glycerol, 1-pentanol, poor activity with 1-butanol, 1-propanol, ethanol, and methanol
-
-
-
additional information
?
-
-
one constitutive enzyme, ADH-MI and one inducible enzyme, ADH-MII
-
-
-
additional information
?
-
Candida sp. N-16
-
one constitutive enzyme, ADH-MI and one inducible enzyme, ADH-MII
-
-
-
additional information
?
-
-
the enzyme exhibits broad substrate specificity towards aliphatic ketones, cycloalkanones, aromatic ketones, and ketoesters
-
-
-
additional information
?
-
-
the enzyme exhibits broad substrate specificity towards aliphatic ketones, cycloalkanones, aromatic ketones, and ketoesters
-
-
-
additional information
?
-
-
no activity with methanol, 2-propanol, and isoamyl alcohol
-
-
-
additional information
?
-
-
when NADH is replaced with NADPH, the reaction rate is reduced by 0.6%
-
-
-
additional information
?
-
-
when NADH is replaced with NADPH, the reaction rate is reduced by 0.6%
-
-
-
additional information
?
-
-
no activity detected with: N-benzyl-2-pyrrolidinone, 2-pyrrolidinone, 3-hexanone, 4-hydroxy-2-butanone, (R)-N-benzyl-3-pyrrolidinol, ethanol, 1,3-propanediol, 1-butanol, 1,4-butanediol, 1,2,3-butanetriol, 1,2,4-butanetriol, acetol, 2-phenyl-1-propanol, 3-phenyl-1-propanol, benzyl alcohol and glycerol. No activity with NADP+ or NADPH
-
-
-
additional information
?
-
-
activity is severely reduced towards aliphatic alcohols of more than 8 carbon atoms for the free enzyme, but not so with immobilized HLAD, exhibiting an activity towards C22 and C24 aliphatic alcohols higher than 50% of the highest value, obtained with C8
-
-
-
additional information
?
-
no activity is detected using 1 mM NADP+
-
-
-
additional information
?
-
no activity with methanol
-
-
-
additional information
?
-
no activity with methanol
-
-
-
additional information
?
-
-
broad substrate specificity
-
-
-
additional information
?
-
-
mutation at the substrate-binding site, or at a dimer interface, alters kinetic properties and protein oligomeric structure, active site flexibility is correlated with subunit interactions 20 A away
-
-
-
additional information
?
-
substrates are a broad range of alkyl alcohols from ethanol to 1-triacontanol
-
-
-
additional information
?
-
substrates are a broad range of alkyl alcohols from ethanol to 1-triacontanol
-
-
-
additional information
?
-
substrates are a broad range of alkyl alcohols from ethanol to 1-triacontanol
-
-
-
additional information
?
-
substrates are a broad range of alkyl alcohols from ethanol to 1-triacontanol
-
-
-
additional information
?
-
-
substrates are a broad range of alkyl alcohols from ethanol to 1-triacontanol
-
-
-
additional information
?
-
-
no activity towards methanol
-
-
-
additional information
?
-
no activity towards methanol
-
-
-
additional information
?
-
no activity towards methanol
-
-
-
additional information
?
-
the NAD+-dependent HvADH1 shows a preference for short-chain alcohols, no activity with methanol
-
-
-
additional information
?
-
-
the NAD+-dependent HvADH1 shows a preference for short-chain alcohols, no activity with methanol
-
-
-
additional information
?
-
the NAD+-dependent HvADH1 shows a preference for short-chain alcohols, no activity with methanol
-
-
-
additional information
?
-
-
differences in the activities of total ADH and class I ADH isoenzyme between cancer liver tissues and healthy hepatocytes may be a factor in ethanol metabolism disorders, which can intensify carcinogenesis
-
-
-
additional information
?
-
1-octanal is no substrate for isozyme ADH1C
-
-
-
additional information
?
-
1-octanal is no substrate for isozyme ADH1C
-
-
-
additional information
?
-
1-octanal is no substrate for isozyme ADH2
-
-
-
additional information
?
-
1-octanal is no substrate for isozyme ADH2
-
-
-
additional information
?
-
1-octanal is no substrate for isozyme ADH4
-
-
-
additional information
?
-
1-octanal is no substrate for isozyme ADH4
-
-
-
additional information
?
-
-
the enzyme does not act on short-chain normal alkyl alcohols, including methanol and ethanol
-
-
-
additional information
?
-
-
the enzyme does not act on short-chain normal alkyl alcohols, including methanol and ethanol
-
-
-
additional information
?
-
-
alcohol dehydrogenase activity may not limit alcohol supply for ester production during ripening
-
-
-
additional information
?
-
-
involvement in the development of male hamster reproductive system
-
-
-
additional information
?
-
mutation at the substrate-binding site, or at a dimer interface, alters kinetic properties and protein oligomeric structure, active site flexibility is correlated with subunit interactions 20 A away
-
-
-
additional information
?
-
mutation at the substrate-binding site, or at a dimer interface, alters kinetic properties and protein oligomeric structure, active site flexibility is correlated with subunit interactions 20 A away
-
-
-
additional information
?
-
-
ADH1 preferrs primary alcohols containing C3-C8 carbons to secondary alcohols such as 2-propanol and 2-butanol. ADH1 possesses specific carboxylate ester-forming activity
-
-
-
additional information
?
-
ADH1 preferrs primary alcohols containing C3-C8 carbons to secondary alcohols such as 2-propanol and 2-butanol. ADH1 possesses specific carboxylate ester-forming activity
-
-
-
additional information
?
-
-
ADH1 preferrs primary alcohols containing C3-C8 carbons to secondary alcohols such as 2-propanol and 2-butanol. ADH1 possesses specific carboxylate ester-forming activity
-
-
-
additional information
?
-
ADH1 preferrs primary alcohols containing C3-C8 carbons to secondary alcohols such as 2-propanol and 2-butanol. ADH1 possesses specific carboxylate ester-forming activity
-
-
-
additional information
?
-
-
no activity with methanol, 1-butanol, glycerol or 2-propanol
-
-
-
additional information
?
-
-
no activity with methanol, 1-butanol, glycerol or 2-propanol
-
-
-
additional information
?
-
methanol, formaldehyde, and acetone are no substrates for HpADH3
-
-
-
additional information
?
-
methanol, formaldehyde, and acetone are no substrates for HpADH3
-
-
-
additional information
?
-
-
enzyme may be involved in the metabolism of dietary wax esters in salmonid fish
-
-
-
additional information
?
-
-
no activity towards methanol, ethanol, 1-propanol, triethylene glycol, polyethylene glycol 400, polyethylene glycol 1000, D-sorbitol, D-sorbose, formaldehyde, acetaldehyde, propionaldehyde, butyraldehyde, and valeraldehyde
-
-
-
additional information
?
-
no activity towards methanol, ethanol, 1-propanol, triethylene glycol, polyethylene glycol 400, polyethylene glycol 1000, D-sorbitol, D-sorbose, formaldehyde, acetaldehyde, propionaldehyde, butyraldehyde, and valeraldehyde
-
-
-
additional information
?
-
no activity towards methanol, ethanol, 1-propanol, triethylene glycol, polyethylene glycol 400, polyethylene glycol 1000, D-sorbitol, D-sorbose, formaldehyde, acetaldehyde, propionaldehyde, butyraldehyde, and valeraldehyde
-
-
-
additional information
?
-
-
broad substrate specificity with a preference for the reduction of ketones and the oxidation of secondary alcohols
-
-
-
additional information
?
-
broad substrate specificity with a preference for the reduction of ketones and the oxidation of secondary alcohols
-
-
-
additional information
?
-
-
substrate specificity and stereospecificity, substrate binding pocket structure of the 3 isozymes, involving Met294, Trp57, and Trp93
-
-
-
additional information
?
-
-
effects of pressure on deuterium isotope effects of yeast alcohol dehydrogenase using alternative substrates
-
-
-
additional information
?
-
-
the enzyme oxidizes alcohols to aldehydes or ketones both for detoxification and metabolic purposes
-
-
-
additional information
?
-
the physiological direction of the catalytic reaction is reduction rather than oxidation
-
-
-
additional information
?
-
the enzyme displays a preference for the reduction of alicyclic, bicyclic and aromatic ketones and alpha-ketoesters, but is poorly active on aliphatic, cyclic and aromatic alcohols, showing no activity on aldehydes
-
-
-
additional information
?
-
-
the enzyme displays a preference for the reduction of alicyclic, bicyclic and aromatic ketones and alpha-ketoesters, but is poorly active on aliphatic, cyclic and aromatic alcohols, showing no activity on aldehydes
-
-
-
additional information
?
-
the enzyme shows no activity on aliphatic linear and branched alcohols, except for a poor activity on 2-propyn-1-ol, 3-methyl-1-butanol and 2-pentanol; however, it shows a discrete activity on aliphatic cyclic and bicyclic alcohols. Benzyl alcohol and 4-bromobenzyl alcohol are not found to be substrates. The S and R enantiomers of a-(trifluoromethyl)benzyl alcohol and methyl and ethyl mandelates show no apparent activity with SaADH. The enzyme shows poor activity on (+/-)-1-phenyl-1-propanol, 1-(1-naphthyl)ethanol and the two enantiomers of 1-(2-naphthyl)ethanol. The enzyme is not active on aliphatic and aromatic aldehydes, and on aliphatic linear, branched and cyclic ketones except for 3-methylcyclohexanone. Catalytic inactivity is observed with acetophenone and (S)-a-(trifluoromethyl)benzyl
-
-
-
additional information
?
-
enzyme displays a preference for the reduction of alicyclic, bicyclic and aromatic ketones and alpha-keto esters, but is poorly active on aliphatic, cyclic and aromatic alcohols, and shows no activity on aldehydes
-
-
-
additional information
?
-
the physiological direction of the catalytic reaction is reduction rather than oxidation
-
-
-
additional information
?
-
the enzyme shows no activity on aliphatic linear and branched alcohols, except for a poor activity on 2-propyn-1-ol, 3-methyl-1-butanol and 2-pentanol; however, it shows a discrete activity on aliphatic cyclic and bicyclic alcohols. Benzyl alcohol and 4-bromobenzyl alcohol are not found to be substrates. The S and R enantiomers of a-(trifluoromethyl)benzyl alcohol and methyl and ethyl mandelates show no apparent activity with SaADH. The enzyme shows poor activity on (+/-)-1-phenyl-1-propanol, 1-(1-naphthyl)ethanol and the two enantiomers of 1-(2-naphthyl)ethanol. The enzyme is not active on aliphatic and aromatic aldehydes, and on aliphatic linear, branched and cyclic ketones except for 3-methylcyclohexanone. Catalytic inactivity is observed with acetophenone and (S)-a-(trifluoromethyl)benzyl
-
-
-
additional information
?
-
the enzyme displays a preference for the reduction of alicyclic, bicyclic and aromatic ketones and alpha-ketoesters, but is poorly active on aliphatic, cyclic and aromatic alcohols, showing no activity on aldehydes
-
-
-
additional information
?
-
enzyme displays a preference for the reduction of alicyclic, bicyclic and aromatic ketones and alpha-keto esters, but is poorly active on aliphatic, cyclic and aromatic alcohols, and shows no activity on aldehydes
-
-
-
additional information
?
-
the enzyme undergoes a substantial conformational change in the apo-holo transition, accompanied by loop movements at the domain interface
-
-
-
additional information
?
-
-
ethanol dehydrogenase activity of Thermoanaerobium brockii is both NAD and NADP linked, reversible, and not inhibited by low levels of reaction products
-
-
-
additional information
?
-
enzyme reduces aldehydes to (R)-alcohols with more than 99.8% enantiomeric excess
-
-
-
additional information
?
-
-
enzyme shows high substrate specificity towards primary aliphatic alcohols, no activity with 2-butanol, tert-butanol, isoamyl alcohol, isobutyl alcohol, 1,6-hexadiol, and mono-, di-, and triethanolamine
-
-
-
additional information
?
-
TADH is a NAD(H)-dependent enzyme and shows a very broad substrate spectrum producing exclusively the (S)-enantiomer in high enantiomeric excess (more than 99%) during asymmetric reduction of ketones
-
-
-
additional information
?
-
ADH exhibits a clear preference for primary alcohols and corresponding aldehydes for aliphatic substrates, in the oxidative direction activity steeply increases with chain length until 1-propanol and then decreases slightly again with growing chain length, alpha,beta-unsaturated ketones like 3-penten-2-one and cyclohexenone are not converted by ADH, almost no conversion of methanol (0.2%) and (+)-carvone (0.4%) is detected
-
-
-
additional information
?
-
TADH is a NAD(H)-dependent enzyme and shows a very broad substrate spectrum producing exclusively the (S)-enantiomer in high enantiomeric excess (more than 99%) during asymmetric reduction of ketones
-
-
-
additional information
?
-
ADH exhibits a clear preference for primary alcohols and corresponding aldehydes for aliphatic substrates, in the oxidative direction activity steeply increases with chain length until 1-propanol and then decreases slightly again with growing chain length, alpha,beta-unsaturated ketones like 3-penten-2-one and cyclohexenone are not converted by ADH, almost no conversion of methanol (0.2%) and (+)-carvone (0.4%) is detected
-
-
-
additional information
?
-
-
preference for reduction of aromatic ketones and alpha-keto esters, and poor activity on aromatic alcohols and aldehydes
-
-
-
additional information
?
-
-
the enzyme transfers the pro-S hydrogen of [4R-(2)H]NADH and exhibits Prelog specificity
-
-
-
additional information
?
-
-
the enzyme transfers the pro-S hydrogen of [4R-(2)H]NADH and exhibits Prelog specificity
-
-
-
additional information
?
-
enzyme selectively reduces the C=O bond of allylic aldehydes/ketones to the corresponding alpha,beta-unsaturated alcohols and also has the capacity of stereoselectively reducing aromatic ketones to (S)-enantioselective alcohols. The enzyme preferentially catalyzes oxidation of allylic/benzyl aldehydes
-
-
-
additional information
?
-
enzyme selectively reduces the C=O bond of allylic aldehydes/ketones to the corresponding alpha,beta-unsaturated alcohols and also has the capacity of stereoselectively reducing aromatic ketones to (S)-enantioselective alcohols. The enzyme preferentially catalyzes oxidation of allylic/benzyl aldehydes
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a primary alcohol + NAD+
an aldehyde + NADH + H+
-
ADH3 is involved in multiple cellular pathways, as diverse as formaldehyde detoxification, retinoid metabolism and NO homeostasis, ADH3 is considered to play only a minor role in hepatic alcohol metabolism because ethanol concentrations rarely exceed 50 mM
-
-
?
allyl alcohol + NAD+
acrolein + NADH
-
-
product is toxic in mouse hepatocytes due to cell protein carbonylation following exposure to crotyl alcohol
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
-
cells with an extra copy of ADH1 display chronological life-span extension. Antioxidant enzymes are induced in 2xADH1 cells. Strains carrying an extra ADH1 copy show extended replicative life span and increased Sir2p activity
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH
-
ADH4 might be involved in biosynthesis of retinoic acid
-
-
r
crotyl alcohol + NAD+
crotonaldehyde + NADH
-
product is toxic in mouse hepatocytes due to cell protein carbonylation following exposure to crotyl alcohol
-
-
?
crotyl alcohol + NAD+
crotonaldehyde + NADH
-
-
product is toxic in mouse hepatocytes due to cell protein carbonylation following exposure to crotyl alcohol
-
?
ethanol + NAD+
acetaldehyde + NADH
-
plays an important role in the metabolism of ethanol
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
chi-ADH plays an important role in the metabolism of long chain alcohols and aldehydes
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
the anodic enzyme form may contribute significantly to alcohol elimination in man, particularly at high concentrations when the other enzyme species are saturated
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
the enzyme plays a significant role in first-pass metabolism of ethanol in human
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
enzyme is responsible for the major ethanol oxidation capacity in the body. The products acetaldehyde and NADH are responsible for the most of the toxic effects and metabolic disturbances produced by ethanol ingestion
-
?
ethanol + NAD+
acetaldehyde + NADH
-
role of the major liver isoenzyme A2 in ethanol metabolism
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
DH3 plays an important role in systemic ethanol metabolism at higher levels of blood ethanol through activation by cytoplasmic solution hydrophobicity
-
-
?
ethanol + NAD+
acetaldehyde + NADH
-
rate-limiting step of the alcoholic fermentation
-
-
?
additional information
?
-
-
one constitutive enzyme, ADH-MI and one inducible enzyme, ADH-MII
-
-
-
additional information
?
-
Candida sp. N-16
-
one constitutive enzyme, ADH-MI and one inducible enzyme, ADH-MII
-
-
-
additional information
?
-
-
activity is severely reduced towards aliphatic alcohols of more than 8 carbon atoms for the free enzyme, but not so with immobilized HLAD, exhibiting an activity towards C22 and C24 aliphatic alcohols higher than 50% of the highest value, obtained with C8
-
-
-
additional information
?
-
-
differences in the activities of total ADH and class I ADH isoenzyme between cancer liver tissues and healthy hepatocytes may be a factor in ethanol metabolism disorders, which can intensify carcinogenesis
-
-
-
additional information
?
-
-
alcohol dehydrogenase activity may not limit alcohol supply for ester production during ripening
-
-
-
additional information
?
-
-
involvement in the development of male hamster reproductive system
-
-
-
additional information
?
-
-
enzyme may be involved in the metabolism of dietary wax esters in salmonid fish
-
-
-
additional information
?
-
-
the enzyme oxidizes alcohols to aldehydes or ketones both for detoxification and metabolic purposes
-
-
-
additional information
?
-
Q4J702
the physiological direction of the catalytic reaction is reduction rather than oxidation
-
-
-
additional information
?
-
Q4J702
the physiological direction of the catalytic reaction is reduction rather than oxidation
-
-
-
additional information
?
-
B2ZRE3
TADH is a NAD(H)-dependent enzyme and shows a very broad substrate spectrum producing exclusively the (S)-enantiomer in high enantiomeric excess (more than 99%) during asymmetric reduction of ketones
-
-
-
additional information
?
-
B2ZRE3
TADH is a NAD(H)-dependent enzyme and shows a very broad substrate spectrum producing exclusively the (S)-enantiomer in high enantiomeric excess (more than 99%) during asymmetric reduction of ketones
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
dependent on, cofactor binding mechanism and conformation from crystal structure analysis
NAD+
-
the monomer consists of a catalytic and a cofactor-binding domain, the cofactor is bound between 2 domains in a cleft
NAD+
specific for NAD+, no activity with NADP+, pro-R stereospecificity for hydrogen transfer
NAD+
-
; strict requirement for NAD(H) as the coenzyme. Critical role of the D37 residue in discriminating NAD(H) from NADP(H)
NAD+
ADH1 preferrs NAD+ 205fold better than NADP+ as cofactor; ADH3 does not react with NADP+
NAD+
-
the binding of NAD+ is kinetically limited by a unimolecular isomerization (corresponding to the conformational change) that is controlled by deprotonation of the catalytic zinc-water to produce a negatively-charged zinc-hydroxide, which can attract the positively-charged nicotinamide ring
NAD+
-
-
285582, 285583, 285584, 285585, 285586, 285587, 285588, 285590, 285591, 285592, 285594, 285595, 285596, 285609, 285610, 285641, 285647, 285648, 285653, 285657, 654743, 655206, 668487, 697215, 697660, 697669
NAD+
-
-
285558, 285641, 285642, 285643, 285644, 285645, 285646, 285649, 655735, 667307, 669148, 695705, 697267, 697658, 697669, 699019
NAD+
NAD+ is prefered over NADP+; NADP+ is prefered over NAD+
NAD+
-
strict requirement for NAD(H) as the coenzyme, no activity with NADP+. The specificity constant value is 6fold higher for NADH than NAD+
NAD+
the enzyme transfers the deuteride to the Si-face of NAD+
NAD+
-
-
285611, 285621, 285625, 677301, 679816, 679883, 681372, 681629, 681763, 682627, 682630, 697839, 720145, 720330
NAD+
-
Adh3 is strictly dependent on NAD+/NADH, and shows no activity with NADP+/NADPH as cofactor
NAD+
-
-
285565, 285566, 285567, 285568, 285569, 285570, 285571, 285572, 285573, 285574, 285575, 285576, 285577, 285578, 285608, 285651, 655197, 655206, 656058, 686331, 691867, 697802, 722073
NADH
-
-
285582, 285583, 285584, 285585, 285586, 285587, 285588, 285589, 285590, 285591, 285592, 285594, 285595, 285596, 285609, 285610, 285641, 285647, 285648, 285653, 285657
NADH
-
-
285565, 285566, 285567, 285568, 285569, 285570, 285571, 285572, 285573, 285574, 285575, 285576, 285577, 285578, 285608, 285651, 656058
NADH
-
; strict requirement for NAD(H) as the coenzyme. Critical role of the D37 residue in discriminating NAD(H) from NADP(H)
NADH
-
strict requirement for NAD(H) as the coenzyme, no activity with NADPH. The specificity constant value is 6fold higher for NADH than NAD+
NADH
strictly required; the specificity constant value is 21-fold higher for NADH than NAD+. No activity with NADP(H)
NADH
-
Adh3 is strictly dependent on NAD+/NADH, and shows no activity with NADP+/NADPH as cofactor
NADH
-
the enzyme transfers the pro-S hydrogen of [4R-(2)H]NADH and exhibits Prelog specificity
NADP+
-
specific for, residues Gly223, Thr224, His225, Leu200, and Lys228 are involved in cofactor binding pocket formation
NADP+
NAD+ is prefered over NADP+; NADP+ is prefered over NAD+
NADPH
-
specific for, residues Gly223, Thr224, His225, Leu200, and Lys228 are involved in cofactor binding pocket formation
additional information
-
crystallographic study of the coenzyme binding mode
-
additional information
-
kinetics of native and modified enzyme with coenzyme analogues
-
additional information
-
kinetic study on the binding of monomeric and polymeric derivatives of NAD+
-
additional information
-
NADP+ shows less than 0.1% of the activity with NAD+
-
additional information
-
the enzyme prefers NAD(H) over NADP(H) as a cofactor
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
CaCl2 and MgCl2 are able to stabilize the enzyme at millimolar concentrations. Ca2+ stabilizes yeast ADH I by preventing the dissociation of the reduced form of the enzyme and by preventing the unfolding of the oxidized form of the enzyme. Ca2+ is fixed by the Asp236 and Glu101 side chains in yeast ADH I
Co2+
Cu2+
Fe2+
KCl
Li+
Mg2+
Mn2+
Na+
Ni2+
selenium
Zinc
Zn2+
additional information
Co2+
-
construction of an active metal-substituted mutant by substituting Zn2+ for Cu2+ or Co2+, which maintain the same configuration as the native zinc ion, but possessing a wider pH range and a lower activity and substrate affinity than the wild-type enzyme, overview
Cu2+
-
construction of an active metal-substituted mutant by substituting Zn2+ for Cu2+ or Co2+, which maintain the same configuration as the native zinc ion, but possessing a wider pH range and a lower activity and substrate affinity than the wild-type enzyme, overview
Fe2+
1 mM, 136% of initial activity; 1 mM, 168% of initial activity
KCl
optimally active with ethanol and 1-propanol at pH 11.0 with 3 M KCl and with 1-butanol at pH 10.0 with 4 M KCl. Catalyzes the reductive reaction optimally at pH 6.0 with 4 M KCl
Mg2+
essential for activity, in the absence of Mg2+ in the kinetic assay no ADH activity is detected
Ni2+
-
activates, the activity using 1,3-propanediol as substrate is highly dependent on the addition of NiCl2, while no change in activity is observed using ethanol in a sample with NiCl2
selenium
-
steady-state fluorescence properties of alcohol dehydrogenase and its selenomethionyl derivative
selenium
-
the effect of significant decrease in intrinsic fluorescence intensity of the enzyme caused by replacement of S atoms of methionine residues to Se is explained on the basis of the analysis of its 3D structure. All selenium atoms are located far from both Trp95 and Trp117 and can not cause their fluorescence quenching. Substitution of S by Se causes enhanced protein absorption in the UV-region. This effect is explained by the formation of Se complex with some groups of protein
Zinc
-
substitution of catalytic and /or noncatalytic zinc ions by cobaltous ions
Zinc
-
from beta1gamma1 and gamma1gamma1 isoenzyme the active-site zinc is extracted much more slowly than from beta1beta1 isoenzyme. Characterization of active-site-specific zinc-depleted and reconstituted cobalt(II) alcohol dehydrogenase
Zinc
KmADH3 appears to belong to the zinc-containing Adh family; KmADH4 appears to belong to the zinc-containing Adh family
Zinc
-
isoenzyme AA-ADH contains 4.3 zinc atoms per dimeric molecule, isoenzyme BB-ADH contains 3.7 zinc atoms per dimeric molecule, isoenzyme AA-ADH contains 4.1 zinc atoms per dimeric molecule
Zinc
-
isoenzyme A2 contains 2.7 mol of zinc per mol of enzyme, isoenzyme b2 contains 1.9 mol of zinc per mol of enzyme, isoenzyme C2 contains 3.2 mol of zinc per mol of enzyme. A and C subunits each contain two atoms of zinc, with at least one being involved catalytically, the b subunit probably contains a single non-catalytic zinc atom
Zinc
-
ADH-1 contains 3.9 mol of zinc per mol of subunit, ADH-2 contains 4.2 mol of zinc per mol of subunit
Zn2+
-
ADH I contains 1 Zn2+ per subunit, while ADH II does not contains any metal ions
Zn2+
1 catalytic zinc ion and 1 structural zinc ion per enzyme subunit
Zn2+
stimulation. Crystal structure of alcohol dehydrogenase domain contains 0.43 Zn atoms per protein monomer
Zn2+
-
2 atoms are included in each 40 kDa subunit, while one of the zinc ions is considered to serve a structural function only, the other zinc ion functions as a Lewis acid and activates the substrate in the active site, which is located in a cleft between the catalytic and the coenzyme binding domain
Zn2+
-
1 catalytic and 1 structural zinc ion per subunit, coordination complex geometry
Zn2+
-
all isozymes, amino acid residues involved in zinc in binding are Cys46, Cys174, His67, Glu68, Asp49, and Thr48, binding mode
Zn2+
-
the catalytic active site zinc ion is bound to Glu69 in the apoenzyme state, but not in the ternary complex state
Zn2+
-
contains a zinc ion which is directly involved in the structural stabilization of enzyme molecule
Zn2+
maximum activity is reached at 0.5 mM Zn2+,Ta1316 ADH is able to tolerate high concentrations of Zn2+
additional information
enzyme contains neither Fe nor other metals, and Fe is not required for the activity, although sequence analysis reveals that ADH1 belongs to the Fe-containing/activated long-chain alcohol dehydrogenases; enzyme contains neither Fe nor other metals, and Fe is not required for the activity, although sequence analysis reveals that ADH1 belongs to the Fe-containing/activated long-chain alcohol dehydrogenases
additional information
enzyme contains neither Fe nor other metals, and Fe is not required for the activity, although sequence analysis reveals that ADH1 belongs to the Fe-containing/activated long-chain alcohol dehydrogenases; enzyme contains neither Fe nor other metals, and Fe is not required for the activity, although sequence analysis reveals that ADH1 belongs to the Fe-containing/activated long-chain alcohol dehydrogenases
additional information
alcohol dehydrogenase activity is stimulated by a range of divalent metal ions, while aldehyde dehydrogenase activity is not
additional information
-
alcohol dehydrogenase activity is stimulated by a range of divalent metal ions, while aldehyde dehydrogenase activity is not
additional information
Mg2+ does not have any effect on activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,4-dioxane
30%, 5–30% inactivation of the initial values following 5 h incubation at 50°C
2-propanol
120–125% activation after incubation for 25 h in the presence of 17% 2-propanol. High concentration (30%) result in enzyme inactivation to 5–30% of the initial values following 5 h incubation at 50°C
3-butylthiolan 1-oxide
-
dead-end inhibitor to the enzyme-cofactor complex, inhibition of oxidation reaction
5-beta-D-ribofuranosylnicotinamide adenine dinucleotide
-
potent and specific inhibitor
5alpha-androstan-17beta-ol-3-one
-
i.e. 5alpha-dihydrotestosterone, allosteric, competitive against substrate cyclohexanone, noncompetitive against NAD+ nd ethanol
acetonitrile
120–125% activation after incubation for 25 h in the presence of 17% acetonitrile. High concentration (30%) result in enzyme inactivation to 5–30% of the initial values following 5 h incubation at 50°C
Biochanin A
-
inhibition of isoenzyme BB-ADH, no inhibition of isoenzyme AA-ADH and TT-ADH
cyanide
-
competitive with nicotinamide nucleotides. NADH increases cyanide-resistance of ADH II
cyclobutyl carbinol
-
complete inhibition in vitro at 890 nM, anti-amoebic activity on trophozoites by growth inhibition of recombinant Escherichia coli cells
cyclopropyl carbinol
-
complete inhibition in vitro at 1820 nM, anti-amoebic activity on trophozoites by growth inhibition of recombinant Escherichia coli cells
daidzein
-
inhibition of isoenzyme BB-ADH, no inhibition of isoenzyme AA-ADH and TT-ADH
genistein
-
inhibition of isoenzyme BB-ADH, no inhibition of isoenzyme AA-ADH and TT-ADH
Glutaraldehyde
-
71% relative activity in the presence of 10 mM glutaraldehyde
N-cyclopentyl-N-cyclobutylformamide
-
inhibits isozyme alphaalpha, complex structure
NO
-
Cys residues contained within the zinc/thiolate active center may be primary sites of NO interaction
o-phenanthroline
-
loses 30% of its activity immediately on addition of o-phenanthroline
p-nitrophenol
-
noncompetitive inhibition of the hydrolysis of p-nitrophenyl octanoate
pyridoxal 5'-phosphate
-
inactivates by modifying its epsilon-amino group, NAD+ protects
S-2-Chloro-3-(imidazol-5-yl)propionate
-
inactivation at pH 8.2, R-2-chloro-3-(imidazol-5-yl)propionate has no effect
sodium dodecylsulfate
1 mM, 3% residual activity; 1 mM, no residual activity
sodium iodoacetate
-
increasing concentrations od sodium iodoacetate produce a slight decrease in activity
tert-butyl hydroperoxide
-
irreversible, inactivation is associated with -SH group oxidation
testosterone
-
inhibition of isoenzyme BB-ADH, no inhibition of isoenzyme AA-ADH and TT-ADH
1,10-phenanthroline
-
inhibition of isoenzyme A2 and C2, no inhibition of isoenzyme B2
1-butyl-3-methylimidazolium tetrafluoroborate
-
5%, 50% inhibition, presumably due to a competition of the BF4- ion with the coenzyme phosphate moiety for the anion-binding site of the enzyme
1-butyl-3-methylimidazolium tetrafluoroborate
-
2 mM, 35% of initial activity; 2 mM, 65% inhibition
4-methoxypyrazole
-
class I ADHs migrate towards cathode on starch gel and are very sensitive to 4-methylpyrazole inhibition, class II ADH migrates slowly towards anode and is less sensitive to 4-methylpyrazole, class II ADH migrates rapidly towards anode and is insensitive to 4-methylpyrazole
4-methoxypyrazole
-
0.1-10 mM, ADH-2 is practically insensitive, ADH-3 is very sensitive
4-Methylpyrazole
-
class III enzyme is completely insensitive to inhibition
4-Methylpyrazole
-
inhibits cell protein carbonylation following exposure to crotyl alcohol
Al3+
1 mM, 14.7% residual activity; 1 mM, 18.9% residual activity
Co2+
1 mM, 51.9% residual activity; 1 mM, 68.7% residual activity
Cu2+
1 mM, 14.0% residual activity; 1 mM, 44.2% residual activity
DMSO
DMSO inhibits isozyme ADH2-catalysed oxidation in an uncompetitive mode and reduction in a mixed mode; DMSO inhibits isozymes ADH1C-catalysed oxidation in an uncompetitive mode and reduction in a mixed mode, no inhibition is detected with isozyme ADH3; DMSO inhibits isozymes ADH4-catalysed oxidation in an uncompetitive mode and reduction in a mixed mode
EDTA
-
67% inhibition of ADH II at 5 mM, 45% inhibition of ADH I at 1 mM, irreversible inhibition, addition of Mg2+ and Zn2+ increase the inhibitory effect
ethanol
ethanol competitively inhibits the oxidation of 1-hydroxymethylpyrene by ADH1C and ADH3; ethanol competitively inhibits the oxidation of 1-hydroxymethylpyrene by ADH4
H2O2
-
inactivation is caused by oxidation of its functional Cys residues, coenzyme protects from inactivation
imidazole
-
pure competitive inhibition towards ethanol and (R)-(+)-phenylethanol
Isobutyramide
-
substrate inhibition, competitive against retinol, noncompetitive against NADH
K+
1 mM, 70.3% residual activity; 1 mM, 82.3% residual activity
Mg2+
1 mM, 0.3% residual activity; 1 mM, 74.3% residual activity
Mn2+
1 mM, 14.3% residual activity; 1 mM, 23.4% residual activity
Ni2+
1 mM, 18.2% residual activity; 1 mM, 72.7% residual activity
Octanoic acid
-
competitive inhibition of the hydrolysis of p-nitrophenyl octanoate
pyrazole
-
pyrazole-sensitive enzyme forms ADH-1, ADH-2, ADH-3 and the pyrazole-insensitive form ADH-An
pyrazole
-
organism has a pyrazole-sensitive isoenzyme and a pyrazole-insensitive enzyme
pyrazole
-
inhibition of isoenzyme A2 and C2. Isoenzyme B2 is insensitive to pyrazole inhibition with trans-2-hexen-1-ol as substrate
pyrazole
-
0.1-10 mM, ADH-2 is practically insensitive, ADH-3 is very sensitive
pyrazole
-
organism has a pyrazole-sensitive isoenzyme and a pyrazole-insensitive enzyme
SDS
-
in the presence of the surfactant the initial reaction rates are consistently lower than in pure buffer at all the surfactant concentrations considered (0.5-50 mM). This effect is mainly due to an increase in the dissociation constant of beta-NAD+ which reaches its maximum value (7.1 mM) at the critical micelle concentration. Above the critical micelle concentration the effect of the surfactant is mainly due to an increase in the Michaels constants of the alcohol, with values of 41 mM for 15 mM SDS and 50 mM for 50 mM SDS
Tween 80
-
competitive, stabilizes the retinoid compounds, elevates the Km values of the substrates, most effective at 0.1% w/v
Zn2+
1 mM, 14.1% residual activity; 1 mM, 30.5% residual activity
additional information
-
no inhibition by 4-chloromercuribenzoate at 0.1 mM and by CuSO4 at 1 mM, poor effects by EDTA, 1,20-phenanthroline, 2-mercaptoethanol, and DTT
-
additional information
-
thiols and dithiols have their main effect, at the enzyme-NAD+-thiol complex level, by competition with alcohol for the catalytic zinc
-
additional information
-
no inhibitory: Triton X-100 at 1%, guanidinium hydrochloride at 0.2 M
-
additional information
-
use of competitive dead-end inhibitors to determine the chemical mechanism of action of yeast alcohol dehydrogenase
-
additional information
the chlorides of Li+, Na+, K+, Ca2+, Mg2+, and Mn2+ do not affect the activity of the enzyme, whereas the sulfate of heavy metal ions such as Fe2+, Co2+, and Cu2+ cause a slight inactivation
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,4-dioxane
significant increases in enzyme activity occurs after 25 h incubation at a concentration of 30%
2-propanol
120–125% activation after incubation for 25 h in the presence of 17% 2-propanol. High concentration (30%) result in enzyme inactivation to 5–30% of the initial values following 5 h incubation at 50°C
Glutaraldehyde
-
treating with 0.5% glutaraldehyde solution, the activity of the immobilized enzyme is at maximum
n-heptane
significant increases in enzyme activity occurs after 25 h incubation at a concentration of 30%
n-hexane
significant increases in enzyme activity occurs after 25 h incubation at a concentration of 30%
S-nitrosoglutathione
-
ADH3-mediated alcohol oxidation is promoted in the presence of S-nitrosoglutathione
TBME
significant increases in enzyme activity occurs after 25 h incubation at a concentration of 30%
acetonitrile
120–125% activation after incubation for 25 h in the presence of 17% acetonitrile. High concentration (30%) result in enzyme inactivation to 5–30% of the initial values following 5 h incubation at 50°C
additional information
-
isonicotinimidylation and methylation increases activity
-
additional information
without heat treatment the AdhC enzyme shows no detectable activity, but after 10 min at higher temperatures the activity is revealed. The highest activity is measured after 10 min at 100°C
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.066
12-oxolauric acid methyl ester
-
wild-type, pH 8.0, 60°C
-
0.25
2-ethoxyethanol
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.3
4-methoxybenzylalcohol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
2.4
iso-propanol
2 mM zinc sulfate in 100 mM glycine-NaOH (pH 10.5) at 65°C
2.8
methyl o-chlorobenzoylformate
65°C, pH 5.5; pH 5.5, 65°C
0.41
(R)-2-butanol
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
37.4
(R)-2-butanol
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.22
(R)-2-pentanol
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
11.7
(R)-2-pentanol
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.012
(S)-2-butanol
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
29.8
(S)-2-butanol
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.07
(S)-2-pentanol
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
8.8
(S)-2-pentanol
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.08
1-butanol
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.6
1-butanol
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.038
1-Heptanol
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.21
1-Heptanol
-
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.67
1-Heptanol
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.035
1-Hexanol
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.04
1-Hexanol
-
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.88
1-Hexanol
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.027
1-Pentanol
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.26
1-Pentanol
-
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.9
1-Pentanol
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.24
1-propanol
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.33
1-propanol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
6.5
1-propanol
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.086
12-hydroxylauric acid methyl ester
-
wild-type, pH 8.0, 60°C
-
0.1
12-hydroxylauric acid methyl ester
-
mutant C257L, pH 8.0, 60°C
-
0.6
2-propanol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
0.14
3-bromobenzylalcohol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
1.2
3-methoxybenzylalcohol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C; in the presence of 5 mM benzylalcohol, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
0.27
3-Pentanol
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.12
4-bromobenzylalcohol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
0.28
4-carboxybenzaldehyde
-
in 50 mM Tris-HCl (pH 7.5) containing 0.2 mM NADH + H+, at 65°C
0.14
4-chloroacetophenone
-
pH 6.0, 37°C, recombinant enzyme expressed from Hansenula polymorpha
0.53
4-chloroacetophenone
-
pH 6.0, 37°C, recombinant enzyme expressed from Saccharomyces cerevisiae
1.11
4-chloroacetophenone
-
pH 6.0, 37°C, recombinant enzyme expressed from Arxula adeninivorans
0.14
4-methoxybenzaldehyde
-
in 50 mM Tris-HCl (pH 7.5) containing 0.2 mM NADH + H+, at 65°C
0.07
4-methoxybenzyl alcohol
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.12
4-methoxybenzyl alcohol
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.3
4-methoxybenzyl alcohol
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.2
acetaldehyde
pH 7.0, temperature not specified in the publication
2.25
acetaldehyde
cosubstrate NADPH, pH 8.0, 60°C
4
acetaldehyde
pH 7.0, temperature not specified in the publication
4.71
acetaldehyde
cosubstrate NADH, pH 8.0, 60°C
28
acetaldehyde
pH 6.0, temperature not specified in the publication
34
acetaldehyde
wild-type, 60°C, pH 6.0, presence of 0.1 mM Zn2+
121
acetaldehyde
alcohol dehydrogenase domain, 60°C, pH 6.0, presence of 0.1 mM Zn2+
0.2
acetophenone
-
pH 6.0, 37°C, recombinant enzyme expressed from Hansenula polymorpha
0.4
acetophenone
-
pH 6.0, 37°C, recombinant enzyme expressed from Arxula adeninivorans
0.66
acetophenone
-
pH 6.0, 37°C, recombinant enzyme expressed from Saccharomyces cerevisiae
0.03
benzaldehyde
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.07
benzaldehyde
-
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.28
benzaldehyde
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.3
benzaldehyde
-
in 50 mM Tris-HCl (pH 7.5) containing 0.2 mM NADH + H+, at 65°C
2 - 3
benzaldehyde
in the presence of 0.25 mM NADH, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
14
benzaldehyde
-
isozyme ADH2, in the presence of 0.25 mM NADH, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
33
benzaldehyde
-
isozyme ADH1, in the presence of 0.25 mM NADH, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
0.12
benzyl alcohol
-
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.26
benzyl alcohol
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.8
benzyl alcohol
-
mutant Y25A/W49F/W167Y, 30°C, pH not specified in the publication
3.1
benzyl alcohol
-
mutant W49F/W167Y, 30°C, pH not specified in the publication
3.8
benzyl alcohol
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
4.2
benzyl alcohol
-
mutant V260A, 30°C, pH not specified in the publication
5.4
benzyl alcohol
-
mutant Y25A/W49F/W167Y/V260A, 30°C, pH not specified in the publication
6
benzyl alcohol
-
mutant W49F/W87F, 30°C, pH not specified in the publication
6.8
benzyl alcohol
-
wild-type, 30°C, pH not specified in the publication
8.2
benzyl alcohol
-
mutant W49F/W167Y/V260A, 30°C, pH not specified in the publication
10.1
benzyl alcohol
-
mutant Y25A/W49F/W87F/V260A, 30°C, pH not specified in the publication
10.9
benzyl alcohol
-
mutant Y25A/W49F/W87F, 30°C, pH not specified in the publication
12.9
benzyl alcohol
-
mutant W49F/W87F/V260A, 30°C, pH not specified in the publication
16.5
benzyl alcohol
-
mutant Y25A, 30°C, pH not specified in the publication
24
benzyl alcohol
in the presence of 2 mM NAD+, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
34
benzyl alcohol
-
isozyme ADH1, in the presence of 2 mM NAD+, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
49
benzyl alcohol
-
isozyme ADH2, in the presence of 2 mM NAD+, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
0.44
benzylalcohol
2 mM zinc sulfate in 100 mM glycine-NaOH (pH 10.5) at 65°C
0.8
benzylalcohol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
0.07
Butyraldehyde
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.13
Butyraldehyde
-
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.27
Butyraldehyde
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.14
Capronaldehyde
-
pH 6.0, 37°C, recombinant enzyme expressed from Arxula adeninivorans
0.22
Capronaldehyde
-
pH 6.0, 37°C, recombinant enzyme expressed from Saccharomyces cerevisiae
0.25
Capronaldehyde
-
pH 6.0, 37°C, recombinant enzyme expressed from Hansenula polymorpha
0.03
Cyclohexanol
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.045
Cyclohexanol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
4.5
Cyclohexanol
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.7
ethanol
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
1.33
ethanol
2 mM zinc sulfate in 100 mM glycine-NaOH (pH 10.5) at 65°C
4.6
ethanol
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
17
ethanol
pH 7.0, temperature not specified in the publication
26
ethanol
pH 7.0, temperature not specified in the publication
39.7
ethanol
pH 7.0, temperature not specified in the publication
49.5
ethanol
pH 7.0, temperature not specified in the publication
66
ethanol
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.26
Isobutyraldehyde
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.33
Isobutyraldehyde
-
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.76
Isobutyraldehyde
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.19
n-Propanol
2 mM zinc sulfate in 100 mM glycine-NaOH (pH 10.5) at 65°C
0.5
NAD+
-
wild type enzyme, at 65°C, in the presence of benzyl alcohol
0.5
NAD+
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.5
NAD+
-
mutant Y25A/W49F/W167Y, 30°C, pH not specified in the publication
0.9
NAD+
-
mutant Y25A/W49F/W87F, 30°C, pH not specified in the publication
1
NAD+
-
mutant Y25A, 30°C, pH not specified in the publication
1.1
NAD+
-
wild-type, 30°C, pH not specified in the publication
1.3
NAD+
-
mutant W49F/W87F, 30°C, pH not specified in the publication
1.8
NAD+
-
mutant W49F/W167Y, 30°C, pH not specified in the publication
4
NAD+
-
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
8.3
NAD+
-
mutant W49F/W167Y/V260A, 30°C, pH not specified in the publication
9.7
NAD+
-
mutant Y25A/W49F/W167Y/V260A, 30°C, pH not specified in the publication
10
NAD+
-
mutant V260A, 30°C, pH not specified in the publication
10.2
NAD+
-
mutant W49F/W87F/V260A, 30°C, pH not specified in the publication
12.4
NAD+
-
mutant enzyme N249Y, at 65°C, in the presence of benzyl alcohol
14.8
NAD+
-
mutant Y25A/W49F/W87F/V260A, 30°C, pH not specified in the publication
50
NAD+
-
Km above 50 mM, mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.008
NADH
-
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.01
NADH
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.013
NADH
-
wild type enzyme, at 65°C, in the presence of benzaldehyde
0.03
NADH
-
in 50 mM Tris-HCl (pH 7.5) containing 0.25 mM benzaldehyde, at 65°C
0.038
NADH
wild-type, 60°C, pH 6.0, presence of 0.1 mM Zn2+
0.062
NADH
alcohol dehydrogenase domain, 60°C, pH 6.0, presence of 0.1 mM Zn2+
0.21
NADH
-
mutant enzyme N249Y, at 65°C, in the presence of benzaldehyde
0.75
NADH
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.4
NADH
cosubstrate acetaldehyde, pH 8.0, 60°C
2.9
p-Methoxybenzaldehyde
-
isozyme ADH1, in the presence of 0.1 mM NADH, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
3.4
p-Methoxybenzaldehyde
in the presence of 0.1 mM NADH, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
5.9
p-Methoxybenzaldehyde
-
isozyme ADH2, in the presence of 0.1 mM NADH, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
6.9
p-methoxybenzyl alcohol
-
isozyme ADH2, in the presence of 2 mM NAD+, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
11
p-methoxybenzyl alcohol
-
isozyme ADH1, in the presence of 2 mM NAD+, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
22
p-methoxybenzyl alcohol
in the presence of 2 mM NAD+, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C
0.19
phenylacetaldehyde
-
pH 6.0, 37°C, recombinant enzyme expressed from Saccharomyces cerevisiae
0.33
phenylacetaldehyde
-
pH 6.0, 37°C, recombinant enzyme expressed from Hansenula polymorpha
0.91
phenylacetaldehyde
-
pH 6.0, 37°C, recombinant enzyme expressed from Arxula adeninivorans
37.55
phenylglyoxylic acid
-
enzyme covalently immobilized to magnetic Fe3O4 nanoparticles via glutaraldehyde
0.009
trans-cinnamaldehyde
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.09
trans-cinnamaldehyde
-
mutant enzyme W95L,, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.23
trans-cinnamaldehyde
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.17
Valeraldehyde
-
pH 6.0, 37°C, recombinant enzyme expressed from Saccharomyces cerevisiae
0.28
Valeraldehyde
-
pH 6.0, 37°C, recombinant enzyme expressed from Arxula adeninivorans
2
Valeraldehyde
-
pH 6.0, 37°C, recombinant enzyme expressed from Hansenula polymorpha
additional information
additional information
-
Km values for the class I isoenzymes with the substrates ethanol, methanol, ethylene glycol, benzyl alcohol, octanol, cyclohexanol and 16-hydroxyhexadecanoic acid
-
additional information
additional information
-
Km-values of active-site Co(II)substituted enzyme
-
additional information
additional information
-
kinetics of native and modified enzyme with coenzyme analogues
-
additional information
additional information
-
kinetics of ethanol oxidation
-
additional information
additional information
-
kinetics of ethanol oxidation
-
additional information
additional information
-
pH-dependence of Km-value
-
additional information
additional information
-
detailed kinetic mechanism, steady-state kinetics for wild-type and mutant enzymes, investigation of pH-dependency
-
additional information
additional information
-
steady-state kinetics, MW 25 kDa
-
additional information
additional information
-
Km for isozymes ADH1B1, ADH1B2, and ADH4 for all retinoid substrates in forward and reverse reaction
-
additional information
additional information
-
Km for isozymes ADH1, and ADH4 for all retinoid substrates in forward and reverse reaction
-
additional information
additional information
-
wild-type and mutant forms of the 3 isozymes, steady-state kinetics, detailed kinetic analysis, at different pH values and temperatures
-
additional information
additional information
-
steady-state kinetics, kinetic mechanism
-
additional information
additional information
-
detailed kinetics, computational analysis of the reaction mechanism
-
additional information
additional information
-
effects of tert-butanol, butyramide, valeramide and capronamide on KM-value for ethanol
-
additional information
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
308
12-oxolauric acid methyl ester
Geobacillus stearothermophilus
-
wild-type, pH 8.0, 60°C
-
1.6
2-ethoxyethanol
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.5
4-methoxybenzylalcohol
Sulfolobus solfataricus
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
1.4
benzylalcohol
Sulfolobus solfataricus
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
9.2
methyl o-chlorobenzoylformate
Sulfolobus acidocaldarius
Q4J702
65°C, pH 5.5; pH 5.5, 65°C
1
(R)-2-butanol
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.7
(R)-2-butanol
Sulfolobus solfataricus
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.1
(R)-2-pentanol
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.9
(R)-2-pentanol
Sulfolobus solfataricus
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.2
(S)-2-butanol
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
4.8
(S)-2-butanol
Sulfolobus solfataricus
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
2.6
(S)-2-pentanol
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
6.7
(S)-2-pentanol
Sulfolobus solfataricus
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
3.1
1-butanol
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
15.1
1-butanol
Sulfolobus solfataricus
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.51
1-Heptanol
Sulfolobus solfataricus
-
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.6
1-Heptanol
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
11.9
1-Heptanol
Sulfolobus solfataricus
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.42
1-Hexanol
Sulfolobus solfataricus
-
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
2
1-Hexanol
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
13.3
1-Hexanol
Sulfolobus solfataricus
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
260.7
1-Octanol
Geobacillus thermodenitrificans
A4IP64, A4ISB9
cosubstrate NADP+, pH 8.0, 60°C
0.53
1-Pentanol
Sulfolobus solfataricus
-
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
2.5
1-Pentanol
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
16.3
1-Pentanol
Sulfolobus solfataricus
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.2
1-propanol
Sulfolobus solfataricus
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
2.5
1-propanol
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
15.7
1-propanol
Sulfolobus solfataricus
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
27.6
12-hydroxylauric acid methyl ester
Geobacillus stearothermophilus
-
wild-type, pH 8.0, 60°C
-
34.3
12-hydroxylauric acid methyl ester
Geobacillus stearothermophilus
-
mutant C257L, pH 8.0, 60°C
-
0.25
2-propanol
Sulfolobus solfataricus
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
1.2
3-bromobenzylalcohol
Sulfolobus solfataricus
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
1.2
3-methoxybenzylalcohol
Sulfolobus solfataricus
-
in the presence of 5 mM benzylalcohol, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
1.4
3-methoxybenzylalcohol
Sulfolobus solfataricus
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
1.5
3-Pentanol
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1.1
4-bromobenzylalcohol
Sulfolobus solfataricus
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
0.7
4-carboxybenzaldehyde
Sulfolobus solfataricus
-
in 50 mM Tris-HCl (pH 7.5) containing 0.2 mM NADH + H+, at 65°C
145
4-chloroacetophenone
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Hansenula polymorpha
230
4-chloroacetophenone
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Saccharomyces cerevisiae
432
4-chloroacetophenone
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Arxula adeninivorans
0.6
4-methoxybenzaldehyde
Sulfolobus solfataricus
-
in 50 mM Tris-HCl (pH 7.5) containing 0.2 mM NADH + H+, at 65°C
0.37
4-methoxybenzyl alcohol
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
2.9
4-methoxybenzyl alcohol
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
16.8
4-methoxybenzyl alcohol
Sulfolobus solfataricus
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
4.6
4-Nitrobenzaldehyde
Sulfolobus solfataricus
-
in 50 mM Tris-HCl (pH 7.5) containing 0.2 mM NADH + H+, at 65°C
53
acetaldehyde
Kluyveromyces marxianus
G3FFC9, V9SCJ1, V9SDP6, V9SFA1
pH 7.0, temperature not specified in the publication
83
acetaldehyde
Geobacillus thermoglucosidasius
A0A0J9X1L6
wild-type, 60°C, pH 6.0, presence of 0.1 mM Zn2+
138.1
acetaldehyde
Geobacillus thermodenitrificans
A4IP64, A4ISB9
cosubstrate NADPH, pH 8.0, 60°C
283
acetaldehyde
Kluyveromyces marxianus
G3FFC9, V9SCJ1, V9SDP6, V9SFA1
pH 7.0, temperature not specified in the publication
350
acetaldehyde
Geobacillus thermoglucosidasius
A0A0J9X1L6
alcohol dehydrogenase domain, 60°C, pH 6.0, presence of 0.1 mM Zn2+
404.8
acetaldehyde
Geobacillus thermodenitrificans
A4IP64, A4ISB9
cosubstrate NADH, pH 8.0, 60°C
211
acetophenone
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Hansenula polymorpha
259
acetophenone
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Saccharomyces cerevisiae
288
acetophenone
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Arxula adeninivorans
0.36
benzaldehyde
Sulfolobus solfataricus
-
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
3.5
benzaldehyde
Sulfolobus solfataricus
-
in 50 mM Tris-HCl (pH 7.5) containing 0.2 mM NADH + H+, at 65°C
11.3
benzaldehyde
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
13.1
benzaldehyde
Sulfolobus solfataricus
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.35
benzyl alcohol
Sulfolobus solfataricus
-
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
3.6
benzyl alcohol
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
20
benzyl alcohol
Sulfolobus solfataricus
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.45
butanol
Saimiri sciureus
-
pyrazole-sensitive enzyme and pyrazole-insensitive enzyme, pH 10.0
0.36
Butyraldehyde
Sulfolobus solfataricus
-
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
19.7
Butyraldehyde
Sulfolobus solfataricus
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C; wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
317
Capronaldehyde
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Arxula adeninivorans
410
Capronaldehyde
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Hansenula polymorpha
576
Capronaldehyde
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Saccharomyces cerevisiae
0.65
Cyclohexanol
Sulfolobus solfataricus
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
1.2
Cyclohexanol
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
12.4
Cyclohexanol
Sulfolobus solfataricus
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.5
ethanol
Sulfolobus solfataricus
-
in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C
3.1
ethanol
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
4.1
ethanol
Sulfolobus solfataricus
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
4.5
ethanol
Kluyveromyces marxianus
G3FFC9, V9SCJ1, V9SDP6, V9SFA1
pH 7.0, temperature not specified in the publication
33
ethanol
Kluyveromyces marxianus
G3FFC9, V9SCJ1, V9SDP6, V9SFA1
pH 7.0, temperature not specified in the publication
142
ethanol
Kluyveromyces marxianus
G3FFC9, V9SCJ1, V9SDP6, V9SFA1
pH 7.0, temperature not specified in the publication
158
ethanol
Kluyveromyces marxianus
G3FFC9, V9SCJ1, V9SDP6, V9SFA1
pH 7.0, temperature not specified in the publication
0.82
Isobutyraldehyde
Sulfolobus solfataricus
-
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
18.1
Isobutyraldehyde
Sulfolobus solfataricus
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
29
Isobutyraldehyde
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.52
NAD+
Sulfolobus solfataricus
-
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1
NAD+
Geobacillus stearothermophilus
-
mutant W49F/W87F/V260A, 30°C, pH not specified in the publication
1.4
NAD+
Geobacillus stearothermophilus
-
mutant W49F/W167Y/V260A, 30°C, pH not specified in the publication
1.9
NAD+
Geobacillus stearothermophilus
-
mutant V260A, 30°C, pH not specified in the publication; mutant Y25A/W49F/W167Y/V260A, 30°C, pH not specified in the publication
2.5
NAD+
Geobacillus stearothermophilus
-
mutant Y25A/W49F/W167Y, 30°C, pH not specified in the publication; mutant Y25A/W49F/W87F/V260A, 30°C, pH not specified in the publication
3
NAD+
Geobacillus stearothermophilus
-
mutant W49F/W87F, 30°C, pH not specified in the publication
3.4
NAD+
Sulfolobus solfataricus
-
wild type enzyme, at 65°C, in the presence of benzyl alcohol
3.4
NAD+
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
3.4
NAD+
Geobacillus stearothermophilus
-
mutant W49F/W167Y, 30°C, pH not specified in the publication
5.1
NAD+
Geobacillus stearothermophilus
-
mutant Y25A, 30°C, pH not specified in the publication
6.3
NAD+
Geobacillus stearothermophilus
-
mutant Y25A/W49F/W87F, 30°C, pH not specified in the publication
21
NAD+
Sulfolobus solfataricus
-
Km above 50 mM, mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
50
NAD+
Sulfolobus solfataricus
-
mutant enzyme N249Y, at 65°C, in the presence of benzyl alcohol
0.38
NADH
Sulfolobus solfataricus
-
mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
4.5
NADH
Sulfolobus solfataricus
-
in 50 mM Tris-HCl (pH 7.5) containing 0.25 mM benzaldehyde, at 65°C
10.3
NADH
Sulfolobus solfataricus
-
wild type enzyme, at 65°C, in the presence of benzaldehyde
10.3
NADH
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
25.3
NADH
Sulfolobus solfataricus
-
mutant enzyme N249Y, at 65°C, in the presence of benzaldehyde
34.8
NADH
Sulfolobus solfataricus
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
1646
NADH
Geobacillus thermodenitrificans
A4IP64, A4ISB9
cosubstrate acetaldehyde, pH 8.0, 60°C
283.1
NADP+
Geobacillus thermodenitrificans
A4IP64, A4ISB9
cosubstrate 1-octanol, pH 8.0, 60°C
3.17
Octanol
Scyliorhinus canicula
P86884
pH and temperature not specified in the publication
202
phenylacetaldehyde
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Saccharomyces cerevisiae
264
phenylacetaldehyde
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Hansenula polymorpha
303
phenylacetaldehyde
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Arxula adeninivorans
0.21
trans-cinnamaldehyde
Sulfolobus solfataricus
-
mutant enzyme W95L,, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
2.1
trans-cinnamaldehyde
Sulfolobus solfataricus
-
wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
18.9
trans-cinnamaldehyde
Sulfolobus solfataricus
-
mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
418
Valeraldehyde
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Saccharomyces cerevisiae
432
Valeraldehyde
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Arxula adeninivorans
528
Valeraldehyde
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Hansenula polymorpha
additional information
additional information
Homo sapiens
-
turnover-numbers for the class I isoenzymes with the substrates ethanol, methanol, ethylene glycol, benzyl alcohol, octanol, cyclohexanol and 16-hydroxyhexadecanoic acid
-
additional information
additional information
Equus caballus
-
Km-values of active-site Co(II)substituted enzyme
-
additional information
additional information
Drosophila melanogaster
-
kinetics of ethanol oxidation
-
additional information
additional information
Drosophila simulans
-
kinetics of ethanol oxidation
-
additional information
additional information
Homo sapiens
-
kcat for isozymes ADH1B1, ADH1B2, and ADH4 for all retinoid substrates in forward and reverse reaction
-
additional information
additional information
Mus musculus
-
kcat for isozymes ADH1, and ADH4 for all retinoid substrates in forward and reverse reaction
-
additional information
additional information
Mus musculus
-
effects of tert-butanol, butyramide, valeramide and capronamide on turnover-number of ethanol
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
67.2
1-Octanol
Geobacillus thermodenitrificans
A4IP64, A4ISB9
cosubstrate NADP+, pH 8.0, 60°C
1228
4700
12-oxolauric acid methyl ester
Geobacillus stearothermophilus
-
wild-type, pH 8.0, 60°C
210506
3.3
methyl o-chlorobenzoylformate
Sulfolobus acidocaldarius
Q4J702
65°C, pH 5.5; pH 5.5, 65°C
42134
450.8
octanal
Geobacillus thermodenitrificans
A4IP64, A4ISB9
cosubstrate NADPH, pH 8.0, 60°C
837
320
12-hydroxylauric acid methyl ester
Geobacillus stearothermophilus
-
wild-type, pH 8.0, 60°C
210505
340
12-hydroxylauric acid methyl ester
Geobacillus stearothermophilus
-
mutant C257L, pH 8.0, 60°C
210505
389
4-chloroacetophenone
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Arxula adeninivorans
6308
434
4-chloroacetophenone
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Saccharomyces cerevisiae
6308
1036
4-chloroacetophenone
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Hansenula polymorpha
6308
0.048
acetaldehyde
Haloferax volcanii
D4GSN2
pH 6.0, temperature not specified in the publication
90
61.4
acetaldehyde
Geobacillus thermodenitrificans
A4IP64, A4ISB9
cosubstrate NADPH, pH 8.0, 60°C
90
71.7
acetaldehyde
Kluyveromyces marxianus
G3FFC9, V9SCJ1, V9SDP6, V9SFA1
pH 7.0, temperature not specified in the publication
90
85.9
acetaldehyde
Geobacillus thermodenitrificans
A4IP64, A4ISB9
cosubstrate NADH, pH 8.0, 60°C
90
450
acetaldehyde
Kluyveromyces marxianus
G3FFC9, V9SCJ1, V9SDP6, V9SFA1
pH 7.0, temperature not specified in the publication
90
392
acetophenone
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Saccharomyces cerevisiae
982
720
acetophenone
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Arxula adeninivorans
982
1055
acetophenone
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Hansenula polymorpha
982
1640
Capronaldehyde
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Hansenula polymorpha
7164
2264
Capronaldehyde
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Arxula adeninivorans
7164
2618
Capronaldehyde
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Saccharomyces cerevisiae
7164
0.072
ethanol
Haloferax volcanii
D4GSN2
pH 11.0, temperature not specified in the publication
69
0.09
ethanol
Kluyveromyces marxianus
G3FFC9, V9SCJ1, V9SDP6, V9SFA1
pH 7.0, temperature not specified in the publication
69
1.3
ethanol
Kluyveromyces marxianus
G3FFC9, V9SCJ1, V9SDP6, V9SFA1
pH 7.0, temperature not specified in the publication
69
3.5
ethanol
Kluyveromyces marxianus
G3FFC9, V9SCJ1, V9SDP6, V9SFA1
pH 7.0, temperature not specified in the publication
69
9.3
ethanol
Kluyveromyces marxianus
G3FFC9, V9SCJ1, V9SDP6, V9SFA1
pH 7.0, temperature not specified in the publication
69
26.7
NAD+
Geobacillus thermodenitrificans
A4IP64, A4ISB9
cosubstrate 1-octanol, pH 8.0, 60°C
7
1176
NADH
Geobacillus thermodenitrificans
A4IP64, A4ISB9
cosubstrate acetaldehyde, pH 8.0, 60°C
8
117.9
NADP+
Geobacillus thermodenitrificans
A4IP64, A4ISB9
cosubstrate 1-octanol, pH 8.0, 60°C
10
156.8
NADP+
Geobacillus thermodenitrificans
A4IP64, A4ISB9
cosubstrate ethanol, pH 8.0, 60°C
10
333
phenylacetaldehyde
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Arxula adeninivorans
769
800
phenylacetaldehyde
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Hansenula polymorpha
769
1063
phenylacetaldehyde
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Saccharomyces cerevisiae
769
264
Valeraldehyde
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Hansenula polymorpha
1481
589
Valeraldehyde
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Saccharomyces cerevisiae
1481
1543
Valeraldehyde
Rhodococcus ruber
-
pH 6.0, 37°C, recombinant enzyme expressed from Arxula adeninivorans
1481
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.035
cyclohexylformamide
pH 7.5, 25°C, wild-type enzyme, versus benzaldehyde
1.7
ethanol
isozyme ADH1C, using 1-hydroxymethylpyrene as substrate
3.3
ethanol
isozyme ADH4, using 1-hydroxymethylpyrene as substrate
1470
ethanol
isozyme ADH3, using 1-hydroxymethylpyrene as substrate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.01
0.03
0.07
-
gene AdhE deletion mutant, cosubstrate NADPH, pH 7.0, 55°C
0.18
after 5.67fold purification, using benzylalcohol as substrate, at 65°C
0.2
0.25
gene AdhE deletion mutant, cosubstrate NADPH, pH 7.0, 55°C
0.3
-
substrates 1,3-propanediol and NAD+, pH 9.0, 60°C, recombinant enzyme, with NiCl2 addition
0.5
-
purified mutant enzyme W95L, using benzyl alcohol as substrate, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
0.62
0.75
purified enzyme, using benzylalcohol as substrate, at 80°C
1.14
1.3
2 - 2.5
-
substrate diacetyl-acetoin, maximal specific activity detected in reduction reaction, 70°C, pH 6.1
2.5
2.6
in Tris-HCl buffer (pH 7.6), 5 mM dithiothreitol, 0.2 mM NADH, and 10 mM acetaldehyde at 65°C
4.03
-
recombinant wild type enzyme, after 6fold purification, at 65°C
4.2
4.5
-
wild type recombinant enzyme, after 450fold purification, at 65°C
5.2
-
mutant recombinant enzyme E97C, after 260fold purification, at 65°C
17.6
crude extract Ta1316 ADH with ethanol as a substrate, at pH 5.0 and 75°C
18.6
-
purified mutant enzyme W95L/N249Y, using benzyl alcohol as substrate, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
43
108
-
substrate butan-2,3-diol, maximal specific activity detected in oxidation reaction, 70°C, pH 8.8
628.7
purified Ta1316 ADH with ethanol as a substrate, at pH 5.0 and 75°C
additional information
0.01
gene AdhE deletion mutant, cosubstrate NADH, pH 7.0, 55°C
0.03
-
gene AdhE deletion mutant, cosubstrate NADH, pH 7.0, 55°C
0.2
-
substrates 1,3-propanediol and NAD+, pH 9.0, 60°C, recombinant enzyme; substrates acetaldehyde and NADH, pH 8.0, 60°C, recombinant enzyme
4.2
-
purified wild type enzyme, using benzyl alcohol as substrate, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C
additional information
-
activity of the 2 isozmyes with various substrates, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
5.7
5.9
6.5
6.7
6.8
7 - 7.5
7.3
7.5
7.8
8.2
8.5
8.5 - 8.8
-
ethanol oxidation, isoenzyme beta2,beta2, beta2,beta1, alpha,beta2 and beta2gamma1
8.5
8.5
8.8
9 - 10
9 - 10
-
substrate: (S)-(-)-1-phenylethanol and 3 mM NAD+ or methyl benzoylformate + NADH
9.5
10
10.4
10.5
10.6
10.8
11
additional information
7.5
-
enzyme covalently immobilized to magnetic Fe3O4 nanoparticles via glutaraldehyde
8.2
-
and a second optimum at pH 10.6, oxidation of ethanol, pyrazole-sensitive enzyme
9.5
-
for the oxidation reaction, ADH activity shows a slight dependence on pH, displaying a broad peak with a maximum around 9.5
10.6
-
and a second optimum at pH 8.2, oxidation of ethanol, pyrazole-sensitive enzyme
11
optimally active with ethanol and 1-propanol at pH 11.0 with 3 M KCl
additional information
-
pH dependence of the reaction mechanism and enzyme-substrate interaction, overview
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 7.5
pH 4.0: about 80% of maximal activity, pH 7.5: about 60% of maximal activity
4 - 8
-
pH 4.0: about 35% of maximal activity, pH 8.0: about 70% of maximal activity
4.9 - 5.8
pH 4.9: about 25% of maximal activity, pH 5.8: about 40% of maximal activity, reduction reaction
5 - 8
-
pH 5.0: about 50% of maximal activity, pH 8.0: about 40% of maximal activity, reduction of phenylacetaldehyde
5.2 - 6.8
Sporotrichum pulverulentum
-
pH 5.2: about 35% of maximal activity, pH 6.8: about 55% of maximal activity, oxidation of ethanol
5.5 - 7.5
pH 5.5: about 35% of maximal activity, pH 7.5: about 55% of maximal activity, reduction of benzaldehyde
6.7 - 8.5
pH 6.7: about 40% of maximal activity, pH 8.5: about 85% of maximal activity, oxidation reaction
7 - 9.6
-
pH 7.0: about 70% of maximal activity, pH 9.6: about 50% of maximal activity, reduction of 2-pentanone
7 - 8
pH 7: 41% of maximal activity, pH 8: 59% of maximal activity
7.2 - 9.2
Sporotrichum pulverulentum
-
pH 7.2: about 50% of maximal activity, pH 9.2: about 60% of maximal activity
7.5 - 10.8
pH 7.5: about 35% of maximal activity, pH 10.8: about 50% of maximal activity, oxidation of 1-hexanol
8 - 12
-
pH 8.0: about 50% of maximal activity, pH 12.0: about 50% of maximal activity, oxidation of 2-phenylethanol
8 - 10.5
-
pH 8.0: about 40% of maximal activity, pH 10.5: about 85% of maximal activity
8 - 12
8.2 - 9.5
-
pH 8.2: about 10% of maximal activity, pH 9.5: about 40% of maximal activity
9 - 12
-
pH 9.0: about 25% of maximal activity, pH 12.0: about 80% of maximal activity, pyrazole-sensitive enzyme
9.5 - 11.5
-
pH 9.5: about 40% of maximal activity, pH 11.5: about 85% of maximal activity, ethanol oxidation enzyme form ADH-3
9.6 - 11.5
-
pH 9.5: about 40% of maximal activity, pH 11.5: about 30% of maximal activity, oxidation of 2-pentanol
10 - 11
-
pH 10.0: about 50% of maximal activity, pH 11.0: about 75% of maximal activity, pyrazole-insensitive enzyme
8 - 12
-
pH 8.0: about 70% of maximal activity, pH 12: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
30
30 - 37
33
35
39
-
recombinant enzyme expressed in Arxula adeninivorans; reductive reaction, recombinant enzyme expressed from Arxula adeninivorans
40
50
55
65
70
75
78
-
the reaction rate increases up to 78°C and then decreases rapidly due to thermal inactivation
80
85
35
-
recombinant enzyme expressed in Hansenula polymorpha; recombinant enzyme expressed in Saccharomyces cerevisiae; reductive reaction, recombinant enzymes expressed from Saccharomyces cerevisiae and Hansenula polymorpha
40
-
enzyme covalently immobilized to magnetic Fe3O4 nanoparticles via glutaraldehyde
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 60
0°C: about 70% of maximal activity, about 45% of maximal activity
10 - 80
-
more than 40% of activity between 40°C and 70°C with all substrates. The enzyme is not capable of reducing acetaldehyde at 80°C, while remaining activity for alcohol oxidation, temperature optimum lies between 50°C to 60°C
10 - 60
Sporotrichum pulverulentum
-
10°C: about 65% of maximal activity, 50°C: about 40% of maximal activity
20 - 50
20 - 85
-
20°C: about 65% of maximal activity, 85°C: about 90% of maximal activity
50 - 80
-
50°C: 45% of maximal activity, 80°C: about 60% of maximal activity
60 - 90
60°C: 75% of maximal activity, 90°C: 75% of maximal activity
65 - 85
70 - 95
70°C: about 65% of maximal activity, 95°C: about 80% of maximal activity
75 - 90
75°C: about 45% of maximal activity, 90°C: about 45% of maximal activity
20 - 50
20°C: about 80% of maximal activity, 50°C: about 55% of maximal activity
20 - 50
-
20°C: about 80% of maximal activity, 50°C: about 60% of maximal activity, reduction of N-benzyl-3-pyrrolidinone
65 - 85
-
65°C: about 60% of maximal activity, 85°C: about 70% of maximal activity
65 - 85
65°C: about 40% of maximal activity, 85°C: about 35% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the activity of the class I ADH isoenzyme is significantly lower in the wall of aortic aneurysm than in healthy aorta
-
ADH3 plays an important role in systemic ethanol metabolism at higher levels of blood ethanol through activation by cytoplasmic solution hydrophobicity
-
the total alcohol dehydrogenase activity is significantly higher in cancer tissues than in healthy colorectum
-
adhA transcription is induced by ethanol or n-propanol, adhA transcription is subject to glucose catabolite repression. Accordingly, both induction of AdhA activity and ethanol utilization are detected only after depletion of glucose
-
isozyme ADH4, the total alcohol dehydrogenase activity is significantly higher in cancer tissues than in healthy esophagus
additional information
-
among all tested classes of ADH isoenzymes, only class I has higher activity in serum of patients with breast cancer in stage IV. The total ADH activity is not significantly higher in patients with breast cancer than in healthy controls. The changes in activity, especially in class I ADH, appear to be caused by isoenzymes being released from the organ damaged by metastatic disease
-
the total ADH activity is significantly higher (44%) among patients with cancer than healthy ones. The activity of class I ADH isoenzymes is elevated only in the serum of patients with metastatic liver cancer. This increase of activity seems to be caused by the enzyme released from liver cancer cells and primary tumors originating in other organs
significantly expressed in ethanol medium; significantly expressed in ethanol medium
Kluyveromyces marxianus DMKU 3-1042
-
significantly expressed in ethanol medium; significantly expressed in ethanol medium
-
during the biological aging of sherry wines, where Saccharomyces bayanus has to grow on ethanol owing to the absence of glucose, this isoenzyme plays a prominent role by converting the ethanol into acetaldehyde and producing NADH in the process. Overexpression of the gene ADH2 (from Saccharomyces cerevisiae) during alcoholic fermentation has no effect on the proteomic profile or the net production of some metabolites associated with glycolysis and alcoholic fermentation such as ethanol, acetaldehyde, and glycerol. However, it affects indirectly glucose and ammonium uptakes, cell growth, and intracellular redox potential, which lead to an altered metabolome
highest ethanol consumption rate in cultures grown on 0.79% w/v ethanol
-
highest ethanol consumption rate in cultures grown on 0.79% w/v ethanol
-
strongly expressed in glycerol medium
-
upregulated during ripening, the enzyme plays a specific role in the regulation of aroma biosynthesis in melon fruit
-
peel and flesh, alcohol dehydrogenase is independent of ethylene modulation
-
the activities of total alcohol dehydrogenase, aldehyde dehydrogenase and class I alcohol dehydrogenase isoenzyme between cancer liver tissues and healthy hepatocytes might be a factor in ethanol metabolism disorders which can intensify carcinogenesis
-
the changes in the carbon metabolism-associated proteins reflect altered patterns of carbon flux in response to changes in ADH activity in transformed plant leaves
-
-
285581, 285582, 285583, 285584, 285585, 285586, 285587, 285588, 285589, 285590, 285591, 285592, 285594, 285595, 285596, 285597, 285609, 285610, 285641, 285647, 285648, 285653, 654743, 655206, 655233, 668487, 685155, 685703, 695889, 697215, 697660, 697669
-
-
285565, 285567, 285568, 285569, 285570, 285571, 285572, 285573, 285574, 285575, 285576, 285577, 285578
-
the activities of total alcohol dehydrogenase, aldehyde dehydrogenase and class I alcohol dehydrogenase isoenzyme between cancer liver tissues and healthy hepatocytes might be a factor in ethanol metabolism disorders which can intensify carcinogenesis
-
the total alcohol dehydrogenase activity is significantly higher in cancer tissues than in healthy liver
-
females show 70% higher hepatic alcohol dehydrogenase activity and display 60% lower voluntary ethanol intake than males. Following ethanol administration (1 g/kg ip), females generate a transient blood acetaldehyde increase with levels that are 2.5fold greater than in males. Castration of males leads to an increase alcohol dehydrogenase activity the appearance of an acetaldehyde burst a reduction of voluntary ethanol intake comparable with that of females
-
total activity of alcohol dehydrogenase is not significantly different in cancer and normal cells. The differences between enzymes of drinkers and nondrinkers in both cancer and healthy tissue are not significant
-
isozymes ADH5 and ADH4, the total alcohol dehydrogenase activity is significantly higher in cancer tissues than in healthy stomach
-
the class III enzyme contributes by far the bulk of the total alcohol dehydrogenase activity
additional information
tissue expression profile of fifth instar larvae, overview
additional information
-
activity of ADH isoenzymes and ALDH in cervical carcinoma and healthy tissues., overview
additional information
-
tissue-specific expression patterns of class I, III, and IV Adh
additional information
-
ADH3 is expressed ubiquitously and with relatively little inter-tissue variation in mammals, in contrast to other ADHs
additional information
-
tissue-specific expression patterns of class I, III, and IV Adh
additional information
-
no expression of ADH5 in lung, epididymis, uterus, ovary, thymus, adrenal, small intestine, heart, eye, muscle, brain, testis, stomach, spleen, and liver
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
KlDH3 and KlADH4 are genes encoding mitochondrial alcohol dehydrogenase activities located within the mitochondria. Ethanol induces the transcription of KlADH4 and, conversely, represses that of KlADH3
KmAdh3 possesses an amino-terminal extension as a mitochondrial targeting sequence; KmAdh4 possesses an amino-terminal extension as a mitochondrial targeting sequence
Kluyveromyces marxianus DMKU 3-1042
-
KmAdh3 possesses an amino-terminal extension as a mitochondrial targeting sequence; KmAdh4 possesses an amino-terminal extension as a mitochondrial targeting sequence
-
additional information
-
detection in the membrane pellet is probably due to cosedimentation of the multimeric enzyme during membrane purification
-
additional information
-
detection in the membrane pellet is probably due to cosedimentation of the multimeric enzyme during membrane purification
-
-
additional information
no activity can be localized in the periplasm
-
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Geobacillus thermoglucosidasius (strain C56-YS93)
Lactococcus lactis subsp. lactis (strain KF147)
Lactococcus lactis subsp. lactis (strain KF147)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
39500
isozyme ADH3, apparent molecular weight deduced from electrophoretic mobility
40000
40500
isozyme ADH1C, apparent molecular weight deduced from electrophoretic mobility; isozyme ADH4, apparent molecular weight deduced from electrophoretic mobility
66000
-
recombinant enzyme expressed from Hansenula polymorpha, gel filtration
70000
72000
74000
80000
86000
99000
alcohol dehydrogenase domain, dynamic light-scattering
116000
140000
150000
160000
190000
gel filtration; gel filtration; gel filtration
40000
isozyme ADH2, apparent molecular weight deduced from electrophoretic mobility; isozyme ADH4, calculated from amino acid sequence
72000
-
recombinant enzyme expressed from Arxula adeninivorans and Saccharomyces cerevisiae, gel filtration
86000
alcohol dehydrogenase domain, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homotetramer
monomer
octamer
tetramer
trimer
additional information
?
x * 37443, ADH1, calculated from sequence; x * 37983, ADH3, calculated from sequence
?
-
x * 37443, ADH1, calculated from sequence; x * 37983, ADH3, calculated from sequence
-
dimer
2 * 48600, alcohol dehydrogenase domain, SDS-PAGE. Unlike the native ADHE, the alcohol dehydrogenase domain alone does not assemble into spirosome structures
dimer
-
2 * 48600, alcohol dehydrogenase domain, SDS-PAGE. Unlike the native ADHE, the alcohol dehydrogenase domain alone does not assemble into spirosome structures
-
dimer
-
2 * 39000, isoenzyme B2, SDS-PAGE; 2 * 43000, isoenzyme A2, SDS-PAGE; 2 * 47000, isoenzyme C2, SDS-PAGE
dimer
-
2 * 41700, enzyme form CM-I: a polypeptide chain + C polypeptide chain, enzyme form CM-II: B-chain + C-chain, enzyme form CM III, homodimer of C chains, SDS-PAGE
dimer
-
2 * 39000, ADH-2, SDS-PAGE; 2 * 40000, ADH-3, SDS-PAGE; 2 * 43000, ADH-1, SDS-PAGE
dimer
-
2 * 31100, enzyme form ADH-II, SDS-PAGE; 2 * 34700, enzyme form ADH-I, SDS-PAGE
dimer
-
2 * 38000, enzyme form ADHII, SDS-PAGE; 2 * 40000, enzyme form ADHI
homotetramer
-
4 * 39570, calculated from sequence; 4 * 40000, SDS-PAGE
-
homotetramer
4 * 37477, calculeted from sequence; 4 * 38000, SDS-PAGE
homotetramer
4 * 36000, Ta1316 ADH, SDS-PAGE; 4 * 36010, Ta1316 ADH, calculated from amino acid sequence
octamer
8 * 45000, SDS-PAGE, 8 * 41664, calculated
tetramer
-
the monomer consista of a catalytic and a cofactor-binding domain, the cofactor is bound between 2 domains in a cleft
tetramer
4 * 48000, SDS-PAGE; 4 * 48000, SDS-PAGE; 4 * 48000, SDS-PAGE; 4 * 49000, SDS-PAGE
tetramer
-
4 * 48000, SDS-PAGE; 4 * 48000, SDS-PAGE; 4 * 48000, SDS-PAGE; 4 * 49000, SDS-PAGE
-
tetramer
4 * 28978, calculated, 4 * 30000, SDS-PAGE; 4 * 28978, calculated from sequence; 4 * 30000, SDS-PAGE
tetramer
-
4 * 27024, ESI-MS analysis; 4 * 28978, calculated, 4 * 30000, SDS-PAGE; 4 * 28978, calculated from sequence; 4 * 29000, SDS-PAGE; 4 * 30000, SDS-PAGE
-
tetramer
-
4 * 37588, calculated from amino acid sequence; 4 * 37591, electrospray mass spectrometry; crosslinking of ADH with dimethylsuberimidate and ethylene glycol bis [succinimidylsuccinate] produces mainly dimers and tetramers, suggesting a dimer of dimers assembly
additional information
-
Adh3 forms a Ni2+-containing homodimer in its active form, crystal structure analysis, larger aggregates are inactive
additional information
-
Adh3 forms a Ni2+-containing homodimer in its active form, crystal structure analysis, larger aggregates are inactive
-
additional information
-
quaternary organization and stability, overview
additional information
-
quaternary organization and stability, overview
-
additional information
tetramer structure results from chemical crosslinking experiments
additional information
-
tetramer structure results from chemical crosslinking experiments
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
additional information
proteolytic modification
sequence contains a N-terminal mitochondrial import sequence of 24 amino acids; sequence contains a N-terminal mitochondrial import sequence of 28 amino acids
proteolytic modification
Kluyveromyces marxianus DMKU 3-1042
-
sequence contains a N-terminal mitochondrial import sequence of 24 amino acids; sequence contains a N-terminal mitochondrial import sequence of 28 amino acids
-
additional information
-
carboxymethylation with sodium iodoacetate
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
multiple anomalous dispersion techniques, X-ray diffraction structure determination and analysis at 1.62 A resolution
-
the zinc-containing enzyme has been crystallized by the sitting-drop vapour-diffusion method using PEG 600 as precipitant. Single orthorhombic crystals with maximum dimensions of 0.4 * 0.4 * 1 mm grow from 0.1 M PIPES pH 6.75 containing 13% PEG 600 and 0.5 mM NADH in approximately four weeks. The crystals diffract to better than 1.5 A using synchrotron radiation and belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 100.7, b = 103.2, c = 67.5 A
-
1 A resolution crystal structures of liver alcohol dehydrogenase in complex with NADH and two inhibitors: dimethyl sulfoxide and isobutyramide
-
10 mg/ml purified double mutant H51Q/K228R in complex with NAD+ and 2,3- or 2,4-difluorobenzyl alcohol, in 50 mM ammonium N-[tris(hydroxymethyl)-methyl]-2-aminoethanesulfonate, pH 7.0, 5°C, 1 mM NAD+, 10 mM 2,3-difluorobenzyl alcohol or 2,4-difluorobenzyl alcohol, equilibrated against increasing concentrations of 2-methyl-2,4-pentanediole, crystal formation at 12% 2-methyl-2,4-pentanediole, X-ray diffraction structure determination and analysis
-
enzyme in complex with trifluoroethanol and without NAD+, X-ray diffraction structure determination and analysis at 2.35 A resolution
structure of the alcohol dehydrogenase domain of the ADHE protein 2.5 A resolution and docking of the aldehyde dehydrogenase domain. The aldehyde dehydrogenase and alcohol dehydrogenase domains of a single ADHE may form dimers with different ADHE monomers rather than both with the same molecule
isozyme alphaalpha in complex with inhibitor N-cyclopentyl-N-cyclobutylformamide, isozyme beta(1)beta(1) in complex with inhibitors N-benzylformamide and N-heptylformamide, and isozyme gamma(2)gamma(2) in complex with inhibitor N-1-methylheptylformamide, X-ray diffraction structure determination and analysis at 1.45-2.5 A resolution, structure modeling
-
purified recombinant N-terminally His-tagged Adh3, hanging drop vapour diffusion method, mixing of 0.002 ml of 80mg/ml protein in 50 mM Tris, pH 7.0, with 0.002 ml of reservoir solution, comprising 0.1 M MES, pH 6.5, 16% w/w PEG 20000, and 0.001 ml of 50 mM CaCl2, 20°C, X-ray diffraction structure determination and analysis
-
enzyme-NADP+-cofactor complex, X-ray diffraction strcuture determination and analysis, computational structure modeling
-
ternary complex of enzyme with NADH and ethylene glycol, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement method
-
three-dimensional model of the enzyme structure suggest that Ca2+ can be displaced by replacing Met-168 by an Arg residue
-
trigonal crystal form alcohol dehydrogenase I: evidence for the existence of Zn ions in the crystal, from 20% PEG 4000, 20% 2-propanol, 0.1 M sodium citrate, pH 5.6, and 1 mM NAD+, X-ray diffraction structure determination and analysis at 3.0 A resolution
-
the crystal structure of the binary complex SaADH2–NADH, determined at 1.75 A resolution, reveals details of the active site providing hints on the structural basis of the enzyme enantioselectivity
-
apoenzyme and ternary complex of enzyme with NADH and 2-ethoxyethanol bound to each subunit, X-ray diffraction structure determination and analysis at 2.3 A resolution
-
crystals are grown in the Advanced Protein Crystallization Facility during the Life and Microgravity Sciences Spacelab mission on the US Space Shuttle. Large diffracting crystals are obtained by dialysis, whereas only poor-quality crystals are obtained by vapour diffusion. The quality of both the microgravity and ground-based crystals is analysed by X-ray diffraction. There is some improvement in terms of size and diffraction resolution limit for the microgravity crystals. The twinning observed in the Earthgrown crystals is also present for those grown in microgravity
-
microbatch method in 100 mM Tris-HCl (pH 7.8), 10 mM dithiotreitol with the same volume of 12% (w/v) PEG 4000, 12% (v/v) 2-propanol, 100 mM sodium citrate (pH 5.6) at 20°C
-
twinned crystals are grown with the sitting drop vapour diffusion method using 2-methyl-2,4-pentanediol (50% v/v), Tris/HCl buffer (150 mM, pH 8.4), and NADH (1 mM), prismatic crystals are grown at 4°C and 20°C by microbatch and free interface diffusion methods with Tris/HCl buffer (130 mM, pH 8.0), NADH (2 mM), polyethyleneglycol 4000 (16% w/v), propan-2-ol or propan-1-ol (16% v/v) in trisodium citrate (100 mM, pH 4.8-5.6)
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 2
5.2 - 6.3
-
purified recombinant enzyme expressed from Saccharomyces cerevisiae, at least 80% of the initial activity is retained after 4 min, 30°C
722888
5.5 - 6.3
-
purified recombinant enzyme expressed from Hansenula polymorpha, at least 80% of the initial activity is retained after 4 min, 30°C
722888
5.8 - 6.6
-
purified recombinant enzyme expressed from Arxula adeninivorans, at least 80% of the initial activity is retained after 4 min, 30°C
722888
6 - 8
-
at pH 6.0 and 8.0, the activity of free ADH decreases dramatically during the incubation, and 90 min later most of the activity is lost, the immobilized form retains 81% of activity at pH 8.0
695705
7 - 9
with 100 mM diphosphate buffer at pH 9.0, the enzyme only exhibits 49% of activity, a 50% decrease is obtained using 50 mM bis-Tris propane buffer at pH 7.0-7.5 and 9.0, whereas at pH 8 and 8.5 only a 10% reduction is found
699249
8 - 9
purified recombinant His-tagged enzyme, 10 min, high stability within this range
722337
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
30 - 55
-
the specific activity of ADH decreases rapidly above 30°C, ADH is almost completely inactive after a 36 min incubation at 55°C
32 - 41
-
more than 80% of maximum activity, recombinant enzyme expressed in Saccharomyces cerevisiae; purified recombinant enzyme expressed from Saccharomyces cerevisiae, at least 80% of the initial activity is retained after 4 min
34 - 38
-
more than 80% of maximum activity, recombinant enzyme expressed in Hansenula polymorpha; purified recombinant enzyme expressed from Hansenula polymorpha, at least 80% of the initial activity is retained after 4 min
35
35 - 60
-
58% of the original activity is retained after incubation of the immobilized enzyme at 35°C for 32 h, free enzyme loses 68% activity over a 60 min incubation at 60°C, whereas immobilized ADH retains 44% over a 60 min incubation at 60°C
38.5 - 42.5
-
more than 80% of maximum activity, recombinant enzyme expressed in Arxula adeninivorans; purified recombinant enzyme expressed from Arxula adeninivorans, at least 80% of the initial activity is retained after 4 min
40
45
50
50 - 60
-
thermal unfolding of ADH is not observed below 60°C while the kinetic deactivation is observed even at 50°C
50
55
56
60
65
65 - 88
-
the single and double mutant are less thermoresistant than the wild type enzyme, displaying a transition temperature of 78 and 88°C, respectively, which are 17 and 7°C lower than that of the wild-type enzyme. At 65°C the single mutant W95L is 10fold less active and the double mutant W95L/N249Y is about 6fold more active than wild type enzyme, the reaction rate catalyzed by the double mutant W95L/N249Y increases more markedly than that of the wild type enzyme up to a temperature of about 83°C and then decreases rapidly due to thermal inactivation. The reaction rate of the single mutant W95L increases more slowly up to about 80°C and then decreases rapidly. At 65°C the single mutant is 10fold less active and the double mutant is about 6fold more active than wild type enzyme.
65
70
70 - 80
-
wild type and mutant enzyme N249Y are stable at 70°C, the mutant enzyme seems more thermoresistant than the wild type enzyme up to a temperature of 80°C, after which its activity decreases abruptly
70
75
80
85 - 90
-
half-life of 3 h at 85°C and 1 h at 90°C, the catalytic efficiency is considerably higher at temperatures below 90°C
85
-
pH 8.0, protein concentration 0.5 mg/ml, 3 h, 50% loss of activity
90
95
98
-
the enzyme maintains 24% of the original catalytic activity after incubation for 30 min
additional information
25
purified recombinant His-tagged enzyme, 10 min, completely stable up to
35
-
HLAD is a mesophilic enzyme whose activity and stability are significantly impaired at temperatures over 35°C
45
-
2 h, free YADH is increasingly deactivated during its incubation with decrease of the enzyme concentration from 3.3 to 0.01 mg/ml because of the dissociation of tetrameric YADH into its subunits
50
-
1 h, 90 mM potassium phosphate buffer, pH 6.5, complete loss of activity
55
-
ADH loses less than 30% of its initial activity after a 36 min incubation at 55°C
55
-
the native enzyme remains completely stable after heating for 3 h at 55°C while the carboxymethylated enzyme loses 10% of activity under the same conditions
55
-
ADH is insensitive to thermal stress at 55°C and remains fully active after a 36 min incubation at 55°C
55
-
60 min, 73% loss of activity of enzyme 1, 10% loss of activity of enzyme 2, 21% loss of activity of enzyme 3
56
-
thermal aggregation occurs at 56°C, the thermal denaturation of ADH is irreversible
60
half-life: 50 min in absence of NAD+, 143 min in presence of 0.01 mM NAD+
60
14 h, more than 50% of initial activity; 14 h, more than 50% of initial activity
60
-
60 min, about 35% loss of activity, soluble enzyme and enzyme covalently immobilized to magnetic Fe3O4 nanoparticles via glutaraldehyde
65
-
60 min, about 80% loss of activity of soluble enzyme, about 55% loss of activity of enzyme covalently immobilized to magnetic Fe3O4 nanoparticles via glutaraldehyde
65
-
pH 8.0, protein concentration 2.5 mg/ml, 16 h, stable. 50% loss of activity after 8 h at protein concentration of 0.5 mg/ml
65
-
at 65°C the half-lives of the native and carboxymethylated enzymes are 9 h and 4 h, respectively
65
-
the activity of the recombinant wild type enzyme slowly decreases to 50% after 16 h at 65°C
65
-
inactivation constant for ADHI: 1.23 per min, inactivation constant for ADH II: 0.13 per min
70
-
purified recombinant enzyme expressed from Hansenula polymorpha, over 80% of the initial activity is retained after 60 min
70
24 h, 76% of initial activity; pH 9.0, 50 mM Tris-HCl, 24% loss of acrtivity
90
half-inactivation temperature is 30 min; half-life 30 min
90
-
at 90°C the specific activity is about three times as high as that measured at 65°C
additional information
-
distinct subunits have different deactivation properties
additional information
-
alpha-cyclodextrin causes thermal stabilization and delays the onset of secondary structural unfolding and aggregation by approx. 10°C and the midpoint temperatures by more than 5°C. alpha-Cyclodextrin diminishes the deactivation of the enzyme, decreasing the deactivation constant by more than 50%, and clearly reveals the stabilization of the enzyme not only structurally but also kinetically at higher temperatures
additional information
-
temperature stability profiles of recombinantly expressed enzymes, overview
additional information
-
effect of salts in the high concentration range on the thermal stability
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ADH immobilized on derived attapulgite nanofibers via glutaraldehyde covalent binding retains higher activity over wider ranges of pH and temperature than those of the free enzyme. After shaking at 125 rpm at 35°C for 32 h, a rapid loss in activity is observed, and almost complete activity of immobilized enzyme is lost in 52 h. The activity of immobilized ADH decreases to 80% of its initial value after four cycles of operation and afterwards gradually decreases with every reuse, but it retains 42% activity after eight cycles for bioreduction of ethyl 3-oxobutyrate.
-
dialysis against 50 mM Tris-HCl buffer, stable after 5 h, 3% loss of activity after 1 day, 82% loss of activity after 6 days
-
does not require the presence of reducing agents to mantain its stability even at high temperature, evidently due to the lack in free cysteines
-
effects of salts on the rate constants of inactivation by heat of alcohol dehydrogenase YADH at 60.0°C. At high concentrations, some salts have stabilizing effects, while others are destabilizing. The effects of salts in the high concentration range examined can be described as follows: (decreased thermal stability) NaClO4, NaI = (C2H5)4NBr, NH4Br, NaBr = KBr = CsBr = (no addition), (CH3)4NBr, KCl, KF, Na2SO4 (increased thermal stability). The decreasing effect of NaClO4 controlls the thermal stability of the enzyme absolutely and is not compensated by the addition of Na2SO4, which stabilizes the enzyme
-
enzyme covalently immobilized to magnetic Fe3O4 nanoparticles via glutaraldehyde shows enhanced thermal stability and good durability in the repeated use after recovered by magnetic separations. Within 7 cycles of usage, the remaining activity is about 100%, 89.15%, 79.42%, 69.50%, 62.80%, 56.48%, and 48.26% of the first use
-
enzyme form ADH I is more stable during purification than enzyme form ADH-II
-
even at 50°C the stabilization effect of lipid membranes on the tertiary and quaternary structures of the liposomal YADH allows the enzyme to form its thermostable complex with NAD+ in liposomes
-
sucrose, glucose, and betaine stabilize ADH substantially while D-ribose and sarcosine destabilize the enzyme
-
the catalytic zinc ions have an important stabilizing effect on the tertiary and quaternary structure of the immobilized enzyme
-
the presence of a second phase of a water-insoluble solvent like hexane or octane has only minor effects on the enzyme, which retains 80% of its activity, allowing the use of these solvents in aqueous/organic mixtures to increase the availability of low-water soluble substrates
the recycling stability of YADH in silica-coated alginate gel beads is found to be increased significantly mainly due to the effective inhibition of enzyme leakage by compact silica film
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1,4-dioxane
2-propanol
Acetone
acetonitrile
dimethylformamide
dioxane
DMSO
dodecane
Ethyl acetate
methyl-tert-butylether
significant increases in enzyme activity occurs after 25 h incubation at a concentration of 30%
n-heptane
n-hexane
significant increases in enzyme activity occurs after 25 h incubation at a concentration of 30%
octane
Pyridine
tert-butylmethyl ether
toluene
additional information
1,4-dioxane
30%, 5–30% inactivation of the initial values following 5 h incubation at 50°C; significant increases in enzyme activity occurs after 25 h incubation at a concentration of 30%
1,4-dioxane
-
30%, 5–30% inactivation of the initial values following 5 h incubation at 50°C
-
2-propanol
120–125% activation after incubation for 25 h in the presence of 17% 2-propanol. High concentration (30%) result in enzyme inactivation to 5–30% of the initial values following 5 h incubation at 50°C
2-propanol
-
120–125% activation after incubation for 25 h in the presence of 17% 2-propanol. High concentration (30%) result in enzyme inactivation to 5–30% of the initial values following 5 h incubation at 50°C
-
acetonitrile
120–125% activation after incubation for 25 h in the presence of 17% acetonitrile. High concentration (30%) result in enzyme inactivation to 5–30% of the initial values following 5 h incubation at 50°C
acetonitrile
-
120–125% activation after incubation for 25 h in the presence of 17% acetonitrile. High concentration (30%) result in enzyme inactivation to 5–30% of the initial values following 5 h incubation at 50°C
-
dimethylformamide
-
50% v/v, 75% remaining activity at 4°C after 100 min, 15% remaining activity after 100 min at 25°C
dimethylformamide
-
50% v/v, 20% remaining activity at 4°C or 25°C after 1-100 min
dioxane
-
50% v/v, 50% remaining activity at 4°C after 100 min, 10% remaining activity after 100 min at 25°C
dioxane
-
50% v/v, about 95% remaining activity at 4°C or 25°C after 1-100 min
DMSO
DMSO is not an ideal substrate-delivering solvent for ADH-catalysed reactions; DMSO is not an ideal substrate-delivering solvent for ADH-catalysed reactions
dodecane
-
active, from 25°C up to 75°C, 3 h, stabilization of the enzyme at elevated temperature
Ethyl acetate
30%, 180% of initial activity; significant increases in enzyme activity occurs after 25 h incubation at a concentration of 30%
Ethyl acetate
-
30%, 180% of initial activity; significant increases in enzyme activity occurs after 25 h incubation at a concentration of 30%
-
n-heptane
30%, 180% of initial activity; significant increases in enzyme activity occurs after 25 h incubation at a concentration of 30%
n-heptane
-
30%, 180% of initial activity; significant increases in enzyme activity occurs after 25 h incubation at a concentration of 30%
-
octane
-
active, from 25°C up to 75°C, 3 h, stabilization of the enzyme at elevated temperature
toluene
-
active, from 25°C up to 75°C, 3 h, stabilization of the enzyme at elevated temperature
additional information
-
Adh3 exhibits tolerance to several organic solvents
-
additional information
enzyme shows high resistance to organic solvents
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
Adh1p is oxidatively modified during ageing and, consequently, its activity becomes reduced
-
688866
among all the cysteine residues, Cys43 is the most susceptible to H2O2 oxidation, and the major oxidation products of this cysteine are Cys-SO2H and Cys-SO3H. The oxidation of Cys43 might be responsible for the inactivation of the enzyme upon H2O2 treatment
-
688657
pronounced oxygen lability at pH 9, even at pH 7, 2 h under air, 80% loss of activity
-
285654
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1 M NaCl in 20 mM Tris-HCl (pH 8.4) in the presence of an equal volume of glycerol, 12 months, no loss of activity
-
-20°C, 10 mM potassium phosphate buffer, pH 7.0, containing 0.5 mM NAD+ without loss of activity for several months
-20°C, in the presence of 50% (v/v) glycerol and at highly concentrated solutions (0.75-1 mg protein/ml), 3 days, 40-50% loss of activity
-20°C, inactive after approximately 2 weeks, storage at -80°C or lyophilization does not improve storage time
-20°C, isoenzyme 2 is stable in 50% ethylene glycol for at least 3 months, isoenzyme 1 and 3 maintain less than 50% of their original activity after 2 weeks
-
15°C, 50 mM sodium phosphate buffer, pH 8.0, half-life of wild-type 7 h, half-life of mutant C257L 17 h
-
4°C, 1 M NaCl in 20 mM Tris-HCl (pH 8.4) in the absence of glycerol, 4 months, 60% loss of activity
-
4°C, 5 mM Na phosphate, pH 7.5, the half-life is 24 h. 0.01 mM ethanol effectively stabilizes for several weeks
-
4°C, 5 mM Na-phosphate, pH 7.5, 50% loss of activity after 1 day. Enzyme can be stabilized for up to 2 weeks by storage in buffer containing 10 mM ethanol
-
4°C, 50 mM sodium phosphate buffer, pH 7.0, 10 mM 2-mercaptoethanol, 10% glycerol, both wild-type and mutant C357L stable for several months
-
4°C, in 3.2 M ammonium sulfate or 50% glycerol, 1 day, rapid loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
128fold to homogeneity by adenosine 5'-monophosphate affinity and Mono-Q ion exchange chromatography
-
2 isozymes from cytosol by DEAE ion exchange, hydroxyl apatite, and gel filtration chromatography, ADH I 35fold, ADH II 21fold
-
DEAE-Sepharose CL-4B column chromatograhy and octyl-Sepharose column chromatography
DEAE-Sepharose Fast Flow column chromatography and G75 gel filtration
-
DEAE-Sepharose Fast Flow column chromatography, Matrex Gel Red A column chromatography, and Blue A column chromatography
-
HiLoad Superdex 200 gel filtration
HiTrap heparin-Sepharose column chromatography, DEAE-Sepharose fast-flow column chromatography, and HiLoad Superdex S-75 gel filtration
-
native (R)-specific alcohol dehydrogenase 37fold from strain IFO10003, by ammonium sulfate fractionation, and anion exchange and hydrophobic interaction chromatography to homogeneity
-
native enzyme from liver by anion exchange and AMP affinity chromatography, and a second different step of anion exchange chromatography
partial
recombinant ADH2 alloenzymes from Escherichia coli by DEAE and AMP or blue Sepharose chromatography, and ultrafiltration
-
recombinant enzyme 1.5fold from Escherichia coli strain BL21 (DE3)
-
recombinant enzyme from Escherichia coli by DEAE ion exchange, 5'-AMP-resin affinity, and Mono Q ion exchange chromatography
-
recombinant His-tagged enzyme by nickel affinity chromatography and gel filtration
-
recombinant His6-tagged enzyme from Echerichia coli strain BL21 (DE3) by nickel affinity chromatography
recombinant isozymes from Escherichia coli strain BL21
reombinant fusion enzyme by glutathione affinity chromatography, cleavage of GST fusion tag by thrombin, further purification of the active enzyme
-
soluble recombinant His6-tagged BmADH protein from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
Toyopearl Butyl 650 S column chromatography, Q Sepharose fast flow column chromatography, Superose 12 prep-grade gel filtration, and TosoHaas G 2000 SWXL gel filtration
-
DEAE-Sepharose CL-4B column chromatograhy and octyl-Sepharose column chromatography
DEAE-Sepharose CL-4B column chromatograhy and octyl-Sepharose column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5-7 genes encoding ADH, DNA and amino acid sequence determination and analysis, polymorphism and allelic frequencies analysis, gene ADH2 possesses 2 allelic forms with Ile308 or Val308, expression of ADH2 alloenzymes in Escherichia coli
-
ADH1 is expressed in recombinant Escherichia coli; ADH3 is expressed in recombinant Escherichia coli
DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme under the control of the strong constitutive Arxula adeninivorans-derived TEF1 promoter in auxotrophic Arxula adeninivorans strain G1214, Hansenula polymorpha strain RB11, and Saccharomyces cerevisiae strainSEY6210, using different expression modules for transformation, evaluation of effeciency, overview. Expression in Arxula adeninivorans is most effective
-
DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli using a rhamnose-inducible system
-
DNA and amino acid sequence determination and analysis, recombinant expression of His6-tagged BmADH protein in Escherichia coli strain BL21 (DE3)
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli DH5alpha cells
expression in Caldicellulosiruptor bescii; expression in Caldicellulosiruptor bescii
expression in Clostridium thermocellum; expression in Clostridium thermocellum DSM 1313
expression in Escherichia coli
expression in Escherichia coli. The correct folding of the AdhC enzyme from hyperthermophilic Pyrococcus furiosus in mesophilic recombinant Escherichia coli is greatly influenced by the cultivation temperature. When grown at temperatures above the optimal growth temperature, Escherichia coli produces heat shock proteins to prevent protein aggregation. Heat shock proteins are known for their chaperonin activity, i.e., they help the protein folding and are responsible for an efficient protein quality control. When heated at 45°C for 2.5 h prior to induction, an increase of the activity is monitored compared to the standard cultivation at 37°C. The fast increase to 42°C yields more active enzyme than the slow increase to 42°C. This suggests that heat shock proteins either assist in the correct folding of the AdhC, or maybe even allow for resolubilization of (partially) denatured molecules. The cultivation at 45°C is not successful
expression in Escherichia coli; expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
expression in Escherichia coli; overexpressed in Escherichia coli
expression of human ADH1 in an in vitro transcription/translation system, N-terminally GST-tagged ADH1 in COS cells and in Escherichia coli
-
expression of isozymes in Escherichia coli strain BL21
expression of rat ADH5 in an in vitro transcription/translation system, GFP-tagged ADH5 in COS cells, but no soluble ADH5 protein from heterologously expression in Escherichia coli cells with expression systems successfully used for other mammalian ADHs, including fused to glutathione-S-transferase
-
gene adh3, sequence comparison, expression of N-terminally His-tagged enzyme in Escherichia coli strains NovaBlue Singles and M15[pREP4]
-
gene ADH3, subcloning in Escherichia coli strain DH5alpha, recombinant expression of His6-tagged enzyme in Echerichia coli strain BL21 (DE3), complementation of the HpADH3 mutant by an HpADH3 expression cassette fused to a strong constitutive promoter, the resulting strain produced a significantly increased amount of ethanol compared to the wild-type strain in a glucose medium, while in a xylose medium, the ethanol production is dramatically reduced in an HpADH3 overproduction strain compared to that in the wild-type strain, semi-quantitative RT-PCR analysis
gene chy1186, overexpression in Escherichia coli strain BL21 (DE3), subcloning in Escherichia coli strain DH5alpha
-
gene encoding for ADH of the haloalkaliphilic archaeon Natronomonas pharaonis, which has a 1,068-bp open reading frame that encodes a protein of 355 amino acids, is cloned into the pET28b vector and is expressed in Escherichia coli
-
gene GmAdh2, quantitative RT-PCR expression analysis, phylogenetic analysis
overexpressed in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of Adh is significantly upregulated in 4-day-old soybean seedlings, in in the root apical meristem, subjected to 2 days of flooding
gene expression is largely induced during ethanol fermentation; gene expression is largely induced during ethanol fermentation; gene expression is largely induced during ethanol fermentation; gene expression is largely induced during ethanol fermentation
isoform ADH3 is significantly expressed in presence of ethanol
isoform ADH4 is significantly expressed in stationary phase and in presence of ethanol
isoform is not expressed at 45°C in glycerol-containing medium and is significantly lower expressed at 45°C than at 30°C in ethanol- and glucose-containing medium
osmotic, cold, or drought stress does not induce expression of Adh2
expression of Adh is significantly upregulated in 4-day-old soybean seedlings, in in the root apical meristem, subjected to 2 days of flooding
expression of Adh is significantly upregulated in 4-day-old soybean seedlings, in in the root apical meristem, subjected to 2 days of flooding
-
-
gene expression is largely induced during ethanol fermentation; gene expression is largely induced during ethanol fermentation; gene expression is largely induced during ethanol fermentation; gene expression is largely induced during ethanol fermentation
gene expression is largely induced during ethanol fermentation; gene expression is largely induced during ethanol fermentation; gene expression is largely induced during ethanol fermentation; gene expression is largely induced during ethanol fermentation
-
-
isoform ADH3 is significantly expressed in presence of ethanol
isoform ADH3 is significantly expressed in presence of ethanol
Kluyveromyces marxianus DMKU 3-1042
-
-
isoform ADH4 is significantly expressed in stationary phase and in presence of ethanol
isoform ADH4 is significantly expressed in stationary phase and in presence of ethanol
Kluyveromyces marxianus DMKU 3-1042
-
-
isoform is not expressed at 45°C in glycerol-containing medium and is significantly lower expressed at 45°C than at 30°C in ethanol- and glucose-containing medium
isoform is not expressed at 45°C in glycerol-containing medium and is significantly lower expressed at 45°C than at 30°C in ethanol- and glucose-containing medium
Kluyveromyces marxianus DMKU 3-1042
-
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H51Q
-
site-directed mutagenesis, shifting of pH dependency, increased activity at pH 8.0, decrease of the rate of isomerization of the enzyme-NAD+ complex, which becomes the limiting step for ethanol oxidation
W54L
-
less active than the wild-type enzyme with ethanol, 1-propanol and 1-butanol. With 1-pentanol and 1-hexanol the mutant enzyme is a better catalyst than the wild-type enzyme
C257L
-
mutation introduced to improve stability under oxidzing conditions. Mutant exhibits prolonged stability and an elevated inactivation temperature
V260A
-
kinetic parameters and temperature dependencies similar to wild-type
W49F/W167Y
-
kinetic parameters and temperature dependencies similar to wild-type
W49F/W167Y/V260A
-
kinetic parameters and temperature dependencies similar to wild-type
W49F/W87F
-
kinetic parameters and temperature dependencies similar to wild-type
W49F/W87F/V260A
-
kinetic parameters and temperature dependencies similar to wild-type
W87A
-
mutation results in a loss of the Arrhenius break seen at 30°C for the wild-type enzyme and an increase in cold lability due to destabilization of the active tetrameric form. Kinetic isotope effects are nearly temperature-independent over the experimental temperature range, and similar in magnitude to those measured above 30°C for the wild-type enzyme
W87F
-
investigation on protein dynamics on the microsecond time scale. Mutant exhibits a fast, temperature-independent microsecond decrease in fluorescence followed by a slower full recovery of the initial fluorescence. The results rule out an ionizing histidine as the origin of the fluorescence quenching. A Trp49-containing dimer interface may act as a conduit for thermally activated structural change within the protein interior
W87F/H43A
-
investigation on protein dynamics on the microsecond time scale. Mutant exhibits a fast, temperature-independent microsecond decrease in fluorescence followed by a slower full recovery of the initial fluorescence. The results rule out an ionizing histidine as the origin of the fluorescence quenching. A Trp49-containing dimer interface may act as a conduit for thermally activated structural change within the protein interior
Y25A
Y25A/W49F/W167Y
-
kinetic parameters and temperature dependencies similar to wild-type
Y25A/W49F/W167Y/V260A
-
kinetic parameters and temperature dependencies similar to wild-type
Y25A/W49F/W87F
-
kinetic parameters and temperature dependencies similar to wild-type
Y25A/W49F/W87F/V260A
-
kinetic parameters and temperature dependencies similar to wild-type
S48T
-
isozyme gamma(2)gamma(2), altered active site structure and inhibitor binding
V141L
-
isozyme gamma(2)gamma(2), altered active site structure and inhibitor binding
A25Y
P47A
site-directed mutagenesis, about 100fold increased activity compared to the wild-type enzyme
P47H
site-directed mutagenesis, about 100fold increased activity compared to the wild-type enzyme
P47Q
site-directed mutagenesis, about 100fold increased activity compared to the wild-type enzyme
G223D/T224I
-
highly reduced activity with NADP+ compared to the wild-type enzyme, wild-type-like activity with NAD+
G223D/T224I/H225N
-
altered cofactor specificity, highly reduced activity with NADP+ compared to the wild-type enzyme, wild-type-like activity with NAD+
P704L/H734R
DELTAA200/A201L
-
highly reduced activity compared to the wild-type enzyme
M294L
E97C
-
shows the same activity but a reduced thermostability with respect to the wild type recombinant protein
N249Y
W95L
-
the mutant displays no apparent activity with short-chain primary and secondary alcohols and poor activity with aromatic substrates and coenzyme, the substitution affects the structural stability of the archaeal ADH, decreasing its thermal stability without relevant changes in secondary structure, optimum pH is at about pH 10
W95L/N249Y
-
the mutant exhibits higher activity but decreased affinity toward aliphatic alcohols, aldehydes as well as NAD+ and NADH compared to the wild type enzyme, optimum pH is at about pH 8.6
additional information
Y25A
-
kinetic parameters and temperature dependencies similar to wild-type
Y25A
-
mutation in the dimer-dimer interface, results in kinetic behavior similar to that of mutantion W87A
A25Y
mutation in the dimer-dimer interface, leads to a more thermostable enzyme and a change in the rate-determining step at low temperature
A25Y
-
mutation in the dimer-dimer interface, leads to a more thermostable enzyme and a change in the rate-determining step at low temperature
-
P704L/H734R
-
mutation leads to ethanol-tolerant phenotype. P704L may affect cofactor-binding directly, while mutation H734R is close to the active site iron atom. Mutant displays a complete loss of NADH-dependent activity with concomitant acquisition of NADPH-dependent activity
P704L/H734R
Ruminiclostridium thermocellum DSM 1237
-
mutation leads to ethanol-tolerant phenotype. P704L may affect cofactor-binding directly, while mutation H734R is close to the active site iron atom. Mutant displays a complete loss of NADH-dependent activity with concomitant acquisition of NADPH-dependent activity
-
M294L
-
7-10fold increase in reactivity, V/Km, with butanol, pentanol and hexanol
N249Y
-
mutant shows increased thermal stability and increased catalytic activity compared to the wild type enzyme
N249Y
-
mutant exhibits increased catalytic activity compared to the wild type enzyme
N249Y
-
shows 7fold higher specific activity compared to the wild type enzyme, is active up to 95°C and more stable than the native enzyme, has acquired an improved resistance to proteolysis by thermolysin and shows a decreased activating effect by treatment with denaturants at moderate concentration
additional information
-
mutations Y25A (at the dimer interface) and V260A (at the cofactor-binding domain) exhibit opposing low-temperature effects on the hydride tunneling step. The distal Y25A increases active-site flexibility, V260A introduces a temperature-dependent equilibration process, and the double mutant (Y25A/V260A) eliminates the temperature-dependent transition sensed by the active-site tryptophan in the presence of V260A. V260A displays a structural change in the active-site environment/solvation
additional information
expression of alcohol dehydrogenase domain alone, a minimal functional unit corresponds to amino acids 459-869
additional information
-
expression of alcohol dehydrogenase domain alone, a minimal functional unit corresponds to amino acids 459-869
additional information
-
expression of alcohol dehydrogenase domain alone, a minimal functional unit corresponds to amino acids 459-869
-
additional information
generation of the ADH3 deletion mutant, complementation of the HpADH3 mutant by an HpADH3 expression cassette fused to a strong constitutive promoter, the resulting strain produced a significantly increased amount of ethanol compared to the wild-type strain in a glucose medium, while in a xylose medium, the ethanol production is dramatically reduced in an HpADH3 overproduction strain compared to that in the wild-type strain, phenotype analysis of DELTAHpADH3 and DELTAHpADH1/DELTAHpADH3 mutants, overview
additional information
-
generation of the ADH3 deletion mutant, complementation of the HpADH3 mutant by an HpADH3 expression cassette fused to a strong constitutive promoter, the resulting strain produced a significantly increased amount of ethanol compared to the wild-type strain in a glucose medium, while in a xylose medium, the ethanol production is dramatically reduced in an HpADH3 overproduction strain compared to that in the wild-type strain, phenotype analysis of DELTAHpADH3 and DELTAHpADH1/DELTAHpADH3 mutants, overview
-
additional information
-
replacement of three mobile loops positioned at the top of the canonical (alpha/beta)8-barrel structure by those from human aldose reductase. Replacement of Loops A and B is sufficient to impart from human aldose reductase activity into AdhD, and the resulting chimera retains the thermostability of the parent enzyme. No active chimeras are observed when the from human aldose reductase loops are grafted into a previously engineered cofactor specificity mutant of AdhD, which displays similar kinetics to from human aldose reductase with the model substrate DL-glyceraldehyde
additional information
-
replacement of three mobile loops positioned at the top of the canonical (alpha/beta)8-barrel structure by those from human aldose reductase. Replacement of Loops A and B is sufficient to impart from human aldose reductase activity into AdhD, and the resulting chimera retains the thermostability of the parent enzyme. No active chimeras are observed when the from human aldose reductase loops are grafted into a previously engineered cofactor specificity mutant of AdhD, which displays similar kinetics to from human aldose reductase with the model substrate DL-glyceraldehyde
-
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Zn2+ withdrawal by inactivation with Chelex 100, reactivation of the apoenzyme by addition of CuSO4, 1 h at 25°C, pH 7.6
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
possible usage of the enzyme in bioindustrial processes and as biosensor
degradation
medicine
synthesis
degradation
expression of AdhB gene in an ldh deletion mutant of Caldicellulosiruptor bescii leads to ethanol production at 75°C, near the ethanol boiling point. The AdhB expressing strain produces ethanol (1.4 mM on Avicel, 0.4 mM on switchgrass) as well as acetate (13.0 mM on Avicel, 15.7 mM on switchgrass). The addition of 40 mM MOPS to the growth medium increases the maximal growth yield of C. bescii by approximately twofold; expression of AdhB gene in an ldh deletion mutant of Caldicellulosiruptor bescii leads to ethanol production at 75°C, near the ethanol boiling point. The AdhE expressing strain produce ethanol (2.3 mM on Avicel, 1.6 mM on switchgrass) and acetate (12.3 mM on Avicel, 15.1 mM on switchgrass). The addition of 40 mM MOPS to the growth medium increases the maximal growth yield of C. bescii by approximately twofold
degradation
-
direct conversion of switchgrass to ethanol without conventional pretreatment of the biomass is accomplished by deletion of lactate dehydrogenase and heterologous expression of a Clostridium thermocellum bifunctional acetaldehyde/alcohol dehydrogenase in Caldicellulosiruptor bescii. Whereas wild-type Caldicellulosiruptor bescii lacks the ability to make ethanol, 70% of the fermentation products in the engineered strain are ethanol (12.8 mM ethanol directly from 2% wt/vol switchgrass) with decreased production of acetate by 38% compared with wild-type
degradation
Ruminiclostridium thermocellum DSM 1237
-
direct conversion of switchgrass to ethanol without conventional pretreatment of the biomass is accomplished by deletion of lactate dehydrogenase and heterologous expression of a Clostridium thermocellum bifunctional acetaldehyde/alcohol dehydrogenase in Caldicellulosiruptor bescii. Whereas wild-type Caldicellulosiruptor bescii lacks the ability to make ethanol, 70% of the fermentation products in the engineered strain are ethanol (12.8 mM ethanol directly from 2% wt/vol switchgrass) with decreased production of acetate by 38% compared with wild-type
-
degradation
-
expression of AdhB gene in an ldh deletion mutant of Caldicellulosiruptor bescii leads to ethanol production at 75°C, near the ethanol boiling point. The AdhB expressing strain produces ethanol (1.4 mM on Avicel, 0.4 mM on switchgrass) as well as acetate (13.0 mM on Avicel, 15.7 mM on switchgrass). The addition of 40 mM MOPS to the growth medium increases the maximal growth yield of C. bescii by approximately twofold
-
degradation
-
expression of AdhB gene in an ldh deletion mutant of Caldicellulosiruptor bescii leads to ethanol production at 75°C, near the ethanol boiling point. The AdhE expressing strain produce ethanol (2.3 mM on Avicel, 1.6 mM on switchgrass) and acetate (12.3 mM on Avicel, 15.1 mM on switchgrass). The addition of 40 mM MOPS to the growth medium increases the maximal growth yield of C. bescii by approximately twofold
-
synthesis
-
enzyme can be used in preparative scale enantioselective oxidation of sec-alcohol in asymmetric reduction of ketones, using acetone and 2-propanol, respectively, as cosubstrates for cofactor-regeneration via a coupled-substrate approach
synthesis
-
production of (S)-1-Phenyl-2-propanol, which is used as an intermediate for the synthesis of amphetamines and as a precursor for anti-hypertensive agents and spasmolytics or anti-epileptics
synthesis
-
production of (S)-4-(3,4-methylenedioxyphenyl)-2-propanol, which is converted to LY300164, an orally active benzodiazepine
synthesis
-
production of (3R,5S)-6-benzyloxy-3,5-dihydroxy-hexanoic acid ethyl ester, which is a key chiral intermediate for anticholesterol drugs that act by inhibition of hydroxy methyl glutaryl coenzyme A reductase
synthesis
-
production of (4S,6S)-5,6-dihydro-4-hydroxy-6-methyl-4H-thieno[2,3b]thiopyran-7,7dioxide, which is an intermediate in the synthesis of the carbonic anhydrase inhibitor trusopt. Trusopt is a novel, topically active treatment for glaucoma
synthesis
-
LSADH catalyzed the enantioselective reduction of some ketones with high enantiomeric excesses: phenyl trifluoromethyl ketone to (S)-1-phenyltrifluoroethanol (>99% e.e.), acetophenone to (R)-1-phenylethanol (99% e.e.), and 2-heptanone to (R)-2-heptanol (>99% e.e.) in the presence of 2-propanol without an additional NADH regeneration system. Therefore, it would be a useful biocatalyst
synthesis
-
enzyme catalyzes the following reactions with Prelog specificity: the reduction of acetophenone, 2,2,2-trifluoroacetophenone, alpha-tetralone, and alpha-methyl and alpha-ethyl benzoylformates to (S)-1-phenylethanol (>99% enantiomeric excess), (R)-alpha-(trifluoromethyl)benzyl alcohol (93% enantiomeric excess), (S)-alpha-tetralol (>99% enantiomeric excess), methyl (R)-mandelate (92% enantiomeric excess), and ethyl (R)-mandelate (95% enantiomeric excess), respectively, by way of an efficient in situ NADH-recycling system involving 2-propanol and a second thermophilic ADH
synthesis
-
yeast alcohol dehydrogenase with its cofactor NAD+ can be stably encapsulated in liposomes composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine. The liposomes are 100 nm in mean diameter, the liposomal ADH and NAD+ concentrations are 2.3 mg/ml and 3.9 mM, respectively. Free ADH is increasingly deactivated during its incubation at 45°C for 2 h with decrease of the enzyme concentration from 3.3 to 0.01 mg/ml because of the dissociation of tetrameric ADH into its subunits. Both liposomal enzyme systems, in presence and absence of NAD+, show stabilities at both 45 and 50°C much higher than those of the free enzyme systems, implying that the liposome membranes stabilize the enzyme tertiary and quaternary structures. The enzyme activity of the liposomes in presence of NAD+ show a stability higher than that in absence of NAD+ with a more remarkable effect of NAD+ at 50°C than at 45°C
synthesis
-
the photochemical and enzymatic synthesis of methanol from formaldehyde with alcohol dehydrogenase and NAD+ photoreduction by the visible-light photosensitization of zinc tetraphenylporphyrin tetrasulfonate in the presence of methylviologen, diaphorase, and triethanolamine is developed
synthesis
enzyme catalyses the reduction of alpha-methyl and alpha-ethyl benzoylformate, and methyl o-chlorobenzoylformate with 100% conversion to methyl (S)-mandelate [17% enantiomeric excess (ee)], ethyl (R)-mandelate (50% ee), and methyl (R)-o-chloromandelate (72% ee), respectively, with an efficient in situ NADH-recycling system which involves glucose and a thermophilic glucose dehydrogenase
synthesis
-
alcohol dehydrogenases represent an important group of biocatalysts due to their ability to stereospecifically reduce prochiral carbonyl compounds; expression of enzyme in auxotrophic Arxula adeninivorans, Hansenula polymorpha, and Saccharomyces cerevisiae strains using yeast ribosomal DNA integrative expression cassettes. Recombinant ADH accumulates intracellularly in all strains tested. The best yields of active enzyme are obtained from A. adeninivorans, with Saccharomyces cerevisiae producing intermediate amounts. Although Hansenula polymorpha is the least efficient producer overall, the product obtained is most similar to the enzyme synthesized by Rhodococcus ruber 219 with respect to its thermostability
synthesis
-
synthesis of the cinnamyl alcohol by means of enzymatic reduction of cinnamaldehyde using alcohol both as an isolated enzyme, and in recombinant Escherichia coli whole cells in an efficient and sustainable one-phase system. The reduction of cinnamaldehyde (0.5 g/l, 3.8 mmol/l) by the isolated enzyme occurrs in 3 h at 50°C with 97% conversion, and yields high purity cinnamyl alcohol (98%) with a yield of 88% and a productivity of 50 g/g enzyme. The reduction of 12.5 g/l (94 mmol/l) cinnamaldehyde by whole cells in 6 h, at 37°C and no requirement of external cofactor occurrs with 97% conversion, 82% yield of 98% pure alcohol and a productivity of 34 mg/g wet cell weight
synthesis
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engineering of a strain of Corynebacterium glutamicum, based on inactivation of the pyruvate dehydrogenase complex, pyruvate:quinone oxidoreductase, transaminase B, and additional overexpression of the IlvBNCD genes, encoding acetohydroxyacid synthase, acetohydroxyacid isomeroreductase, and dihydroxyacid dehydratase, for the production of isobutanol from glucose under oxygen deprivation conditions by inactivation of L-lactate and malate dehydrogenases, implementation of ketoacid decarboxylase from Lactococcus lactis, alcohol dehydrogenase 2 (ADH2) from Saccharomyces cerevisiae, and expression of the pntAB transhydrogenase genes from Escherichia coli. The resulting strain produces isobutanol with a substrate-specific yield (YP/S) of 0.60 mol per mol of glucose. Chromosomally encoded alcohol dehydrogenase AdhA rather than the plasmid-encoded ADH2 from Saccharomyces cerevisiae is involved in isobutanol formation, and overexpression of the corresponding AdhA gene increases the YP/S to 0.77 mol of isobutanol per mol of glucose. Inactivation of the malic enzyme significantly reduces the YP/S, indicating that the metabolic cycle consisting of pyruvate and/or phosphoenolpyruvate carboxylase, malate dehydrogenase, and malic enzyme is responsible for the conversion of NADH + H+ to NADPH + H+. In fed-batch fermentations with an aerobic growth phase and an oxygen-depleted production phase, the most promising strain produces about 175 mM isobutanol, with a volumetric productivity of 4.4 mM per h, and shows an overall YP/S of about 0.48 mol per mol of glucose in the production phase
synthesis
synthetic pathway for n-butanol production from acetyl coenzyme at 70°C, using beta-ketothiolase Thl, 3-hydroxybutyryl-CoA dehydrogenase Hbd, and 3-hydroxybutyryl-CoA dehydratase Crt from Caldanaerobacter subterraneus subsp. tengcongensis, trans-2-enoyl-CoA reductase Ter from Spirochaeta thermophila and bifunctional aldehyde dehydrogenase AdhE and and butanol dehydrogenase in vitro. n-Butanol is produced at 70°C, but with different amounts of ethanol as a coproduct, because of the broad substrate specificities of AdhE, Bad, and Bdh. A reaction kinetics model, validated via comparison to in vitro experiments, is used to determine relative enzyme ratios needed to maximize n-butanol production. By using large relative amounts of Thl and Hbd and small amounts of Bad and Bdh, >70% conversion to n-butanol is observed in vitro, but with a 60% decrease in the predicted pathway flux
synthesis
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semi-preparative biocatalysis at 60°C using the stabilized mutant C257L, employing butyraldehyde for in situ cofactor regeneration with only catalytic amounts of NAD+, yields up to 23% conversion of omega-hydroxy lauric acid methyl ester to omega-oxo lauric acid methyl ester after 30 min
synthesis
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recombinant enzyme activity can be improved by coexpression of archaeal chaperones (i.e., gamma-prefoldin and thermosome). Ricinoleic acid biotransformation activity of recombinant Escherichia coli expressing Micrococcus luteus alcohol dehydrogenase and the Pseudomonas putida KT2440 Baeyer-Villiger monooxygenase improves significantly with coexpression of gamma-prefoldin or recombinant themosome originating from the deep-sea hyperthermophile archaea Methanocaldococcus jannaschii. The degree of enhanced activity is dependent on the expression levels of the chaperones
synthesis
engineering of Klebsiella pneumoniae to produce 2-butanol from crude glycerol as a sole carbon source by expressing acetolactate synthase (IlvH), keto-acid reducto-isomerase (IlvC) and dihydroxyacid dehydratase (IlvD) from Klebsiella pneumoniae, and alpha-oxoisovalerate decarboxylase (Kivd) and alcohol dehydrogenase (AdhA) from Lactococcus lactis. The engineered strain produce 2-butanol (160 mg/l) from crude glycerol. Elimination of the 2,3-butanediol pathway by inactivating alpha-acetolactate decarboxylase (Adc) further improves the yield of 2-butanol from 160 to 320 mg/l
synthesis
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simplified production scheme for isobutanol based on a cell-free immobilized enzyme system. Immobilized enzymes keto-acid decarboxylase (KdcA) and alcohol dehydrogenase (ADH) plus formate dehydrogenase (FDH) for NADH recycle in solution produce isobutanol titers 8 to 20 times higher than the highest reported titers with Saccharomyces cerevisiae on a mol/mol basis. Conversion rates and low protein leaching are achieved by covalent immobilization on methacrylate resin. The enzyme system without in situ removal of isobutanol achieves a 55% conversion of ketoisovaleric acid to isobutanol at a concentration of 0.135 mol isobutanol produced for each mol ketoisovaleric acid consumed
synthesis
enhancement of ethanol production capacity of Clostridium thermocellum by transferring pyruvate decarboxylase and alcohol dehydrogenase genes of the homoethanol pathway from Zymomonas mobilis. Both transferring pyruvate decarboxylase and alcohol dehydrogenase are functional in Clostridium thermocellum, but the presence of and alcohol dehydrogenase severely limits the growth of the recombinant strains, irrespective of the presence or absence of the pyruvate decarboxylase gene. The recombinant strain shows two-fold increase in pyruvate carboxylase activity and ethanol production when compared with the wild type strain; expression of pyruvate decarboxylase and alcohol dehydrogenase in Clostridium thermocellum DSM 1313. Though both enzymes are functional in Clostridium thermocellum, the presence of alcohol dehydrogenase severely limits the growth of the recombinant strains, irrespective of the presence or absence of the pyruvate decarboxylase gene
synthesis
construction of an enzyme-immobilized bioanode that can operate at high temperatures. The catalytic current for ethanol oxidation at Ru complex-modified electrodes increases at 80°C up to 12fold compared with room temperature
synthesis
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in order to increase production of isobutanol, 2-oxoacid decarboxylase (KDC) and alcohol dehydrogenase (ADH) are expressed in Saccharomyces cerevisiae to enhance the endogenous activity of the Ehrlich pathway. Overexpression Ilv2, which catalyzes the first step in the valine synthetic pathway, and deletion of the PDC1 gene encoding a major pyruvate decarboxylase alters the abundant ethanol flux via pyruvate. Along with modification of culture conditions, the isobutanol titer is elevated 13fold, from 11 mg/l to 143 mg/l, and the yield is 6.6 mg/g glucose
synthesis
overexpression of the adhB gene results in a significant increase in the ethanol level
synthesis
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alpha-ketoisovalerate decarboxylase Kivd from Lactococcus lactis combined with alcohol dehydrogenase Adh3 from Zymomonas mobilis are the optimum candidates for 3-methyl-1-butanol production in Corynebacterium glutamicum. The recombinant strain produces 0.182 g/l of 3-methyl-1-butanol and 0.144 g/l of isobutanol after 12 h of incubation. Further inactivation of the E1 subunit of pyruvate dehydrogenase complex gene (aceE) and lactic dehydrogenase gene (ldh) improves the 3-methyl-1-butanol titer to 0.497 g/l after 12 h of incubation
synthesis
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deletion of the hypoxanthine phosphoribosyltransferase gene in ethanol tolerant strain adhE*(EA), carrrying mutation P704L/H734R in the alcohol dehydrogenase gene, and deletion of lactate dehydrogenase (ldh) to redirect carbon flux towards ethanol reults in a strain producing 30% more ethanol than wild type on minimal medium. The engineered strain retains tolerance to 5% v/v ethanol, resulting in an ethanol tolerant platform strain
synthesis
construction of a synthetic pathway for bioalcohol production at 70°C by insertion of the gene for alcohol dehydrogenase AdhA into the archaeon Pyrococcus furiosus. The engineered strain converts glucose to ethanol via acetate and acetaldehyde, catalyzed by the host-encoded aldehyde ferredoxin oxidoreductase AOR and heterologously expressed AdhA, in an energy-conserving, redox-balanced pathway. The AOR/AdhA pathway also converts exogenously added aliphatic and aromatic carboxylic acids to the corresponding alcohol using glucose, pyruvate, and/or hydrogen as the source of reductant. By heterologous coexpression of a membrane-bound carbon monoxide dehydrogenase, CO is used as a reductant for converting carboxylic acids to alcohols
synthesis
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protocol for the synthesis of [4R-(2)H]NADH with high yield by enzymatic oxidation of 2-propanol-d(8)
synthesis
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engineering of a strain of Corynebacterium glutamicum, based on inactivation of the pyruvate dehydrogenase complex, pyruvate:quinone oxidoreductase, transaminase B, and additional overexpression of the IlvBNCD genes, encoding acetohydroxyacid synthase, acetohydroxyacid isomeroreductase, and dihydroxyacid dehydratase, for the production of isobutanol from glucose under oxygen deprivation conditions by inactivation of L-lactate and malate dehydrogenases, implementation of ketoacid decarboxylase from Lactococcus lactis, alcohol dehydrogenase 2 (ADH2) from Saccharomyces cerevisiae, and expression of the pntAB transhydrogenase genes from Escherichia coli. The resulting strain produces isobutanol with a substrate-specific yield (YP/S) of 0.60 mol per mol of glucose. Chromosomally encoded alcohol dehydrogenase AdhA rather than the plasmid-encoded ADH2 from Saccharomyces cerevisiae is involved in isobutanol formation, and overexpression of the corresponding AdhA gene increases the YP/S to 0.77 mol of isobutanol per mol of glucose. Inactivation of the malic enzyme significantly reduces the YP/S, indicating that the metabolic cycle consisting of pyruvate and/or phosphoenolpyruvate carboxylase, malate dehydrogenase, and malic enzyme is responsible for the conversion of NADH + H+ to NADPH + H+. In fed-batch fermentations with an aerobic growth phase and an oxygen-depleted production phase, the most promising strain produces about 175 mM isobutanol, with a volumetric productivity of 4.4 mM per h, and shows an overall YP/S of about 0.48 mol per mol of glucose in the production phase
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synthesis
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engineering of Klebsiella pneumoniae to produce 2-butanol from crude glycerol as a sole carbon source by expressing acetolactate synthase (IlvH), keto-acid reducto-isomerase (IlvC) and dihydroxyacid dehydratase (IlvD) from Klebsiella pneumoniae, and alpha-oxoisovalerate decarboxylase (Kivd) and alcohol dehydrogenase (AdhA) from Lactococcus lactis. The engineered strain produce 2-butanol (160 mg/l) from crude glycerol. Elimination of the 2,3-butanediol pathway by inactivating alpha-acetolactate decarboxylase (Adc) further improves the yield of 2-butanol from 160 to 320 mg/l
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synthesis
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LSADH catalyzed the enantioselective reduction of some ketones with high enantiomeric excesses: phenyl trifluoromethyl ketone to (S)-1-phenyltrifluoroethanol (>99% e.e.), acetophenone to (R)-1-phenylethanol (99% e.e.), and 2-heptanone to (R)-2-heptanol (>99% e.e.) in the presence of 2-propanol without an additional NADH regeneration system. Therefore, it would be a useful biocatalyst
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synthesis
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alcohol dehydrogenases represent an important group of biocatalysts due to their ability to stereospecifically reduce prochiral carbonyl compounds; expression of enzyme in auxotrophic Arxula adeninivorans, Hansenula polymorpha, and Saccharomyces cerevisiae strains using yeast ribosomal DNA integrative expression cassettes. Recombinant ADH accumulates intracellularly in all strains tested. The best yields of active enzyme are obtained from A. adeninivorans, with Saccharomyces cerevisiae producing intermediate amounts. Although Hansenula polymorpha is the least efficient producer overall, the product obtained is most similar to the enzyme synthesized by Rhodococcus ruber 219 with respect to its thermostability
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synthesis
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alcohol dehydrogenases represent an important group of biocatalysts due to their ability to stereospecifically reduce prochiral carbonyl compounds; expression of enzyme in auxotrophic Arxula adeninivorans, Hansenula polymorpha, and Saccharomyces cerevisiae strains using yeast ribosomal DNA integrative expression cassettes. Recombinant ADH accumulates intracellularly in all strains tested. The best yields of active enzyme are obtained from A. adeninivorans, with Saccharomyces cerevisiae producing intermediate amounts. Although Hansenula polymorpha is the least efficient producer overall, the product obtained is most similar to the enzyme synthesized by Rhodococcus ruber 219 with respect to its thermostability
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synthesis
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enzyme can be used in preparative scale enantioselective oxidation of sec-alcohol in asymmetric reduction of ketones, using acetone and 2-propanol, respectively, as cosubstrates for cofactor-regeneration via a coupled-substrate approach
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synthesis
Ruminiclostridium thermocellum DSM 1237
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deletion of the hypoxanthine phosphoribosyltransferase gene in ethanol tolerant strain adhE*(EA), carrrying mutation P704L/H734R in the alcohol dehydrogenase gene, and deletion of lactate dehydrogenase (ldh) to redirect carbon flux towards ethanol reults in a strain producing 30% more ethanol than wild type on minimal medium. The engineered strain retains tolerance to 5% v/v ethanol, resulting in an ethanol tolerant platform strain
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synthesis
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overexpression of the adhB gene results in a significant increase in the ethanol level
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synthesis
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enzyme catalyses the reduction of alpha-methyl and alpha-ethyl benzoylformate, and methyl o-chlorobenzoylformate with 100% conversion to methyl (S)-mandelate [17% enantiomeric excess (ee)], ethyl (R)-mandelate (50% ee), and methyl (R)-o-chloromandelate (72% ee), respectively, with an efficient in situ NADH-recycling system which involves glucose and a thermophilic glucose dehydrogenase
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synthesis
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construction of an enzyme-immobilized bioanode that can operate at high temperatures. The catalytic current for ethanol oxidation at Ru complex-modified electrodes increases at 80°C up to 12fold compared with room temperature
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synthesis
Zymomonas mobilis subsp. mobilis ATCC 31821
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enhancement of ethanol production capacity of Clostridium thermocellum by transferring pyruvate decarboxylase and alcohol dehydrogenase genes of the homoethanol pathway from Zymomonas mobilis. Both transferring pyruvate decarboxylase and alcohol dehydrogenase are functional in Clostridium thermocellum, but the presence of and alcohol dehydrogenase severely limits the growth of the recombinant strains, irrespective of the presence or absence of the pyruvate decarboxylase gene. The recombinant strain shows two-fold increase in pyruvate carboxylase activity and ethanol production when compared with the wild type strain; expression of pyruvate decarboxylase and alcohol dehydrogenase in Clostridium thermocellum DSM 1313. Though both enzymes are functional in Clostridium thermocellum, the presence of alcohol dehydrogenase severely limits the growth of the recombinant strains, irrespective of the presence or absence of the pyruvate decarboxylase gene
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